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PubMed2006

Effects of pigeon pea and plantain starches on the compressional, mechanical, and disintegration properties of paracetamol tablets.

A study has been made of the effects of pigeon pea starch obtained from the plant Cajanus cajan (L) Millisp. (family Fabaceae) and plantain starch obtained from the unripe fruit of Musa paradisiaca L. (family Musaceae) on the compressional, mechanical, and disintegration properties of paracetamol tablets in comparison with official corn starch BP. Analysis of compressional properties was done by using density measurements, and the Heckel and Kawakita equations, whereas the mechanical properties of the tablets were evaluated by using tensile strength (T--a measure of bond strength) and brittle fracture index (BFI--a measure of lamination tendency). The ranking for the mean yield pressure, P(y), for the formulations containing the different starches was generally corn < pigeon pea < plantain starch while the ranking for P(k), an inverse measure of the amount of plasticity, was pigeon pea < plantain < corn starch, which indicated that formulations containing corn starch generally exhibited the fastest onset of plastic deformation, whereas those formulations containing pigeon pea starch exhibited the highest amount of plastic deformation during tableting. The tensile strength of the tablets increased with increase in concentration of the starches while the Brittle Fracture Index decreased. The ranking for T was pigeon pea > plantain > corn starch while the ranking for BFI was corn > plantain > pigeon pea starch. The bonding capacity of the formulations was in general agreement with the tensile strength results. The disintegration time (DT) of the formulation increased with concentration of plantain and corn starches but decreased with concentration of pigeon pea starch. The general ranking of DT values was plantain < pigeon pea < corn starch. Notably, formulations containing pigeon pea starch exhibited the highest bond strength and lowest brittleness, suggesting the usefulness of pigeon pea starch in producing strong tablets with minimal lamination tendency. Plantain starch, on the other hand, would be more useful where faster disintegration of tablet is desired. The results show that the starches could be useful in various formulations depending on the intended use of the tablets with the implication that the experimental starches can be developed for commercial purposes.

Acetaminophen↗

PubMed2004

Vicilin and convicilin are potential major allergens from pea.

BACKGROUND: Allergic reactions to pea (Pisum sativum) ingestion are frequently associated with lentil allergy in the Spanish population. Vicilin have been described as a major lentil allergen. OBJECTIVE: To identify the main IgE binding components from pea seeds and to study their potential cross-reactivity with lentil vicilin. METHODS: A serum pool or individual sera from 18 patients with pea allergy were used to detect IgE binding proteins from pea seeds by immunodetection and immunoblot inhibition assays. Protein preparations enriched in pea vicilin were obtained by gel filtration chromatography followed by reverse-phase high-performance liquid chromatography (HPLC). IgE binding components were identified by means of N-terminal amino acid sequencing. Complete cDNAs encoding pea vicilin were isolated by PCR, using primers based on the amino acid sequence of the reactive proteins. RESULTS: IgE immunodetection of crude pea extracts revealed that convicilin (63 kDa), as well as vicilin (44 kDa) and one of its proteolytic fragments (32 kDa), reacted with more than 50% of the individual sera tested. Additional proteolytic subunits of vicilin (36, 16 and 13 kDa) bound IgE from approximately 20% of the sera. The lentil vicilin allergen Len c 1 strongly inhibited the IgE binding to all components mentioned above. The characterization of cDNA clones encoding pea vicilin has allowed the deduction of its complete amino acid sequence (90% of sequence identity to Len c 1), as well as those of its reactive proteolytic processed subunits. CONCLUSIONS: Vicilin and convicilin are potential major allergens from pea seeds. Furthermore, proteolytic fragments from vicilin are also relevant IgE binding pea components. All these proteins cross-react with the major lentil allergen Len c 1.

Adolescent↗

PubMed2004

Effect of field pea level on intake, digestion, microbial efficiency, ruminal fermentation, and in situ disappearance in beef steers fed growing diets.

Effects of increasing level of field pea (variety: Profi) on intake, digestion, microbial efficiency, and ruminal fermentation were evaluated in beef steers fed growing diets. Four ruminally and duodenally cannulated crossbred beef steers (367+/-48 kg initial BW) were used in a 4 x 4 Latin square. The control diet consisted of 50% corn, 23% corn silage, 23% alfalfa hay, and 4% supplement (DM basis). Treatments were field pea replacing corn at 0, 33, 67, or 100%. Diets were formulated to contain a minimum of 12% CP, 0.62% Ca, 0.3% P, and 0.8% K (DM basis). Each period was 14 d long. Steers were adapted to the diets for 9 d. On d 10 to 14, intakes were measured. Field pea was incubated in situ, beginning on d 10, for 0, 2, 4, 8, 12, 16, 24, 36, 48, 72, and 96 h. Bags were inserted in reverse order, and all bags were removed at 0 h. Ruminal fluid was collected and pH recorded at -2, 0, 2, 4, 6, 8, 10, and 12 h after feeding on d 13. Duodenal samples were taken for three consecutive days beginning on d 10 in a manner that allowed for a collection to take place every other hour over a 24-h period. Linear, quadratic, and cubic contrasts were used to compare treatments. There were no differences in DMI (12.46 kg/d, 3.16% BW; P > 0.46). Ruminal dry matter fill (P = 0.02) and mean ruminal pH (P = 0.009) decreased linearly with increasing field pea level. Ruminal ammonia-N (P < 0.001) and total VFA concentrations (P = 0.01) increased linearly with increasing field pea level. Total-tract disappearance of OM (P = 0.03), N (P = 0.01), NDF (P = 0.02), and ADF (P = 0.05) increased linearly with an increasing field pea level. There were no differences in total-tract disappearance of starch (P = 0.35). True ruminal N disappearance increased linearly (P < 0.001) with increasing field pea level. There were no differences in ruminal disappearance of OM (P = 0.79), starch (P = 0.77), NDF (P = 0.21), or ADF (P = 0.77). Treatment did not affect microbial efficiency (P = 0.27). Field pea is a highly digestible, nutrient-dense legume grain that ferments rapidly in the rumen. Because of their relatively high level of protein, including field peas in growing diets will decrease the need for protein supplementation. Based on these data, it seems that field pea is a suitable substitute for corn in growing diets.

Ammonia↗

PubMed2006

The influence of dietary field peas (Pisum sativum L.) on pig performance, carcass quality, and the palatability of pork.

An experiment was conducted to test the hypothesis that field peas may replace soybean meal in diets fed to growing and finishing pigs without negatively influencing pig performance, carcass quality, or pork palatability. Forty-eight pigs (initial average BW 22.7 +/- 1.21 kg) were allotted to 1 of 3 treatments with 2 pigs per pen. There were 8 replications per treatment, 4 with barrows and 4 with gilts. The treatments were control, medium field peas, and maximum field peas. Pigs were fed grower diets for 35 d, early finisher diets for 35 d, and late finisher diets for 45 d. Pigs receiving the control treatment were fed corn-soybean meal diets. All diets fed to pigs receiving the medium field peas treatment contained 36% field peas and varying amounts of corn; soybean meal was also included in the grower and the early finisher diets fed to pigs on this treatment. In contrast, no soybean meal was included in diets fed to pigs on the maximum field peas treatment, and field peas were included at concentrations of 66, 48, and 36% in the grower, early finisher, and late finisher diets, respectively. Pig performance was monitored within each phase and for the entire experimental period. At the conclusion of the experiment, carcass composition, carcass quality, and the palatability of pork chops and pork patties were measured. Results showed that there were no effects of dietary treatments on ADFI, ADG, or G:F. Likewise, there were no differences in carcass composition among the treatment groups, but gilts had larger (P = 0.001) and deeper (P = 0.003) LM, less backfat (P = 0.007), and a greater (P = 0.002) lean meat percentage than barrows. The pH and marbling of the LM, and the 10th rib backfat were not influenced by treatment, but there was a trend (P = 0.10) for more marbling in barrows than in gilts. The subjective color scores (P = 0.003) and the objective color score (P = 0.06) indicated that dietary field peas made the LM darker and more desirable. Pork chops from pigs fed field peas also had less (P = 0.02) moisture loss compared with chops from pigs fed the control diet. Treatment or sex did not influence palatability of pork chops or pork patties. In conclusion, field peas may replace all of the soybean meal in diets fed to growing and finishing pigs without negatively influencing pig performance, carcass composition, carcass quality, or pork palatability.

Animal Feed↗

PubMed1997

Milk production and intake of lactating cows fed raw or extruded peas.

Primiparous (n = 9) and multiparous (n = 18) Holstein cows averaging 584 +/- 15 kg of body weight (mean +/- SE) were allotted at 2 wk postpartum to nine groups (3 primiparous and 6 multiparous) of 3 cows each to determine the effects of pea extrusion on ruminal degradability and milk production. Cows were fed a total mixed diet based on timothy silage and concentrate for ad libitum intake. The experiment was carried out between wk 4 and 15 of lactation. Cows within each group were assigned randomly to isonitrogenous and isoenergetic concentrates based on corn plus soybean meal, raw peas, or extruded peas. Extrusion of peas increased the ruminal degradability of starch but had no effect on the ruminal degradability of crude protein. Cows fed extruded peas had higher dry matter intakes and plasma urea N concentrations than did those fed soybean meal; no differences were detected between cows fed extruded and raw peas. Production of 4% fat-corrected milk and milk composition generally were similar for cows fed the various diets. Digestibilities of dry matter and N were higher for cows fed extruded peas than for cows fed soybean meal or raw peas. These data suggest that peas can substitute for soybean meal as the protein source in diets of early lactation cows without adverse effects on production and that, in this study, the extrusion of peas had no beneficial effect on milk production.

Animal Feed↗

PubMed1996

The enhancement of the nutritive value of peas for broiler chickens: an evaluation of micronization and dehulling processes.

The effects of dehulling and micronization (infrared heating) on the nutritive value of three cultivars (Impala, Radley, and Sirius) of peas (Pisum sativum) varying in coat color for broiler chickens were studied. Dehulling increased (P < or = 0.05) protein and starch contents and decreased (P < or = 0.05) fiber content of peas. Also, the concentrations of most amino acids slightly increased (P > or = 0.05). Micronization slightly changed (P > or = 0.05) the chemical composition of peas. Moisture, protein, fiber and phosphorus contents marginally decreased. The concentrations of aspartic acid, glutamic acid, isoleucine, lysine, cystine, threonine, and tyrosine decreased (P < or = 0.05), whereas that of methionine slightly increased (P > or = 0.05). Lysine concentration was decreased by 2.7%. The TMEn and average true AA availability values determined with adult cockerels were improved (P < or = 0.05) by micronization, but the availabilities of lysine were decreased by 11.3, 4.4, and 2.0% for Impala, Radley and Sirius, respectively. The decrease was significant (P < or = 0.05) for Impala and Radley but not significant for Sirius peas. Application of micronization resulted in a significant (P < or = 0.05) improvement in AMEn, apparent protein digestibility (APD), and starch digestibility. The increments ranged from 19.4 to 31.3, 8.5 to 33.6, and 12.2 to 22.3% for AMEn, APD, and starch digestibility, respectively. In contrast, dehulling had little or no effect on AMEn (3.0 and 4.9%), APD (-1.8 and -4.2%) and starch digestibility (2.0 and 1.3%) values of Impala (yellow-seeded) and Radley (green-seeded) peas but significantly (P < or = 0.05) improved the AMEn (24.1%), APD (26.8%), and starch digestibility (12.1%) values of Sirius (brown-seeded) peas. Chick performance was evaluated in a 2-wk trial. Birds fed micronized peas grew faster and had better feed conversion (P < or = 0.05) than birds fed untreated peas and the wheat-soybean control diet. Addition of lysine to the diet containing micronized peas further improved (P > or = 0.05) weight gains and feed conversion of broiler chicks. Dehulling only improved (P < or = 0.05) the performance of birds fed Sirius peas.

Amino Acids↗

PubMed2004

Composition and in vitro digestibility of raw versus cooked white- and colour-flowered peas.

Ten pea cultivars (four white-flowered, Pisum sativum ssp. hortense, and six colour-flowered, Pisum sativum ssp. arvense) grown in Latvia were analyzed and tested in in vitro experiments, as raw and cooked seeds. The colour-flowered (CF) had a greater proportion of hulls and a higher acid detergent fibre (ADF) content than white-flowered (WF) pea seeds (10.7 vs. 8.2% and 92.2 vs. 84.5 g/kg dry matter (DM), respectively). Three out of six CF varieties had a significantly greater amount of protein bound to neutral detergent fibre (NDF) than WF peas. The tannin content was higher in CF than in WF peas (8.46 vs. 0.37 g/kg DM). In vitro protein and amino acid digestibility was about 8% higher in WF than in CF varieties. Cooking decreased the tannin content in CF peas (8.46 vs. 5.51 g/kg DM) but had no effect on in vitro protein digestibility. Heat treatment reduced significantly trypsin inhibitor activity and amount of protein bound to NDF in CF and WF varieties (from 6.50 to 0.52 and from 6.54 to 0.46 trypsin inhibitor units (TIU)/mg DM; from 1.250 to 0.831 and 0.761 to 0.209 g N/100 g NDF, respectively). However, the protein bound to NDF content in pea DM increased in CF and decreased in WF varieties (from 1.525 to 2.145 and from 0.913 to 0.502 g N/kg DM, respectively). Cooking resulted in an increased NDF content over two times in both CF and WF pea seeds (from 122 to 259 and from 120 to 262 g/kg DM, respectively). The results suggest that colour-flowered pea may be considered as an interesting dietary alternative to white-flowered pea since cooking removes trypsin inhibitor activity (TIA), decreases tannins, and increases dietary fibre contents.

Color↗

PubMed2002

Muscle and liver protein metabolism in rats fed raw or heat-treated pea seeds.

Raw or extruded pea (Pisum sativum, cv. Ballet) diets with or without supplementary amino acids were fed for 15 days to young growing rats and the effects on tissue weights, liver and muscle protein metabolism and hormone levels monitored. Body weight gain, liver and gastrocnemius muscle weights and protein contents were reduced and some key hormones altered when rats were fed unsupplemented raw pea diets. This appeared to be a result of amino acid deficiencies in the diet, the action of antinutritional factors and the refractory nature of the reserve proteins and other seed components. However, this did not in itself improve the nutritional performance of the rats due to the overriding effects of the amino acid deficiencies in the pea diets. After supplementation, extruded peas supported much higher rates of growth and skeletal muscle deposition than did supplemented raw peas. Despite this, the weight gains remained less than achieved on a high quality control diet. Protein synthesis and degradation rates in skeletal muscles and total protein contents were similar to control values. The lower growth rate did not appear to be due to impaired deposition of skeletal muscle. Deposition of other body components, possibly lipids, may have been lowered by supplemented extruded pea diets. Liver protein levels were reduced in rats fed supplemented raw peas and blood corticosterone was elevated. In conclusion, extrusion treatment of peas in combination with amino acid supplementation appeared to abolish the negative effects of peas on skeletal muscle deposition.

Journal Article↗

PubMed2003

Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1).

BACKGROUND: Serologic cross-reactivity among legumes has been described; however, it is rarely clinically significant. In this study 3 patients with a history of anaphylaxis to pea are described who subsequently had symptoms after ingestion of peanut. OBJECTIVE: We investigated whether the peanut-related symptoms were due to cross-reactivity between pea and peanut proteins. METHODS: Peanut-related symptoms were documented according to case history or double-blind, placebo-controlled food challenge results. Skin prick tests were performed, and specific IgE levels were determined for pea and peanut with the CAP system FEIA. IgE-binding proteins in pea and peanut were identified by using immunoblot analysis. Cross-reactivity was studied by means of immunoblot and ELISA inhibition studies with whole extracts and purified allergens. RESULTS: Peanut-related symptoms consisted of oral symptoms in all patients, with additional urticaria and dyspnea or angioedema in 2 patients. All patients had a positive skin prick test response and an increased IgE level to pea and peanut. Immunoblotting revealed strong IgE binding to mainly vicilin in pea extract and exclusively to Ara h 1 in crude peanut extract. Immunoblot and ELISA inhibition studies with crude extracts, as well as purified proteins, showed that IgE binding to peanut could be inhibited by pea but not or only partially the other way around. CONCLUSION: Clinically relevant cross-reactivity between pea and peanut does occur. Vicilin homologues in pea and peanut (Ara h 1) are the molecular basis for this cross-reactivity.

Allergens↗

PubMed2003

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.

Activation of Raf-1 suppresses integrin activation, potentially through the activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2). However, bulk ERK1/2 activation does not correlate with suppression. PEA-15 reverses suppression of integrin activation and binds ERK1/2. Here we report that PEA-15 reversal of integrin suppression depends on its capacity to bind ERK1/2, indicating that ERK1/2 function is indeed required for suppression. Mutations in either the death effector domain or C-terminal tail of PEA-15 that block ERK1/2 binding abrogated the reversal of integrin suppression. Furthermore, we used ERK/p38 chimeras and site-directed mutagenesis to identify ERK1/2 residues required for binding PEA-15. Mutations of residues that precede the alphaG helix and within the mitogen-activated protein kinase insert blocked ERK2 binding to PEA-15, but not activation of ERK2. These ERK2 mutants blocked the ability of PEA-15 to reverse suppression of integrin activation. Thus, PEA-15 regulation of integrin activation depends on its binding to ERK1/2. To directly test the role of ERK1/2 localization in suppression, we enforced membrane association of ERK1 and 2 by joining a membrane-targeting CAAX box sequence to them. Both ERK1-CAAX and ERK2-CAAX were membrane-localized and suppressed integrin activation. In contrast to suppression by membrane-targeted Raf-CAAX, suppression by ERK1/2-CAAX was not reversed by PEA-15. Thus, ERK1/2 are the Raf effectors for suppression of integrin activation, and PEA-15 reverses suppression by binding ERK1/2.

Amino Acid Motifs↗

PubMed2004

The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions.

ERK2 nuclear-cytoplasmic distribution is regulated in response to hormones and cellular state without the requirement for karyopherin-mediated nuclear import. One proposed mechanism for the movement of ERK2 into the nucleus is through a direct interaction between ERK2 and nucleoporins present in the nuclear pore complex. Previous reports have attributed regulation of ERK2 localization to proteins that activate or deactivate ERK2, such as the mitogen-activated protein (MAP) kinase kinase MEK1 and MAP kinase phosphatases. Recently, a small non-catalytic protein, PEA-15, has also been demonstrated to promote a cytoplasmic ERK2 localization. We found that the MAP kinase insert in ERK2 is required for its interaction with PEA-15. Consistent with its recognition of the MAP kinase insert, PEA-15 blocked activation of ERK2 by MEK1, which also requires the MAP kinase insert to interact productively with ERK2. To determine how PEA-15 influences the localization of ERK2, we used a permeabilized cell system to examine the effect of PEA-15 on the localization of ERK2 and mutants that have lost the ability to bind PEA-15. Wild type ERK2 was unable to enter the nucleus in the presence of an excess of PEA-15; however, ERK2 lacking the MAP kinase insert largely retained the ability to enter the nucleus. Binding assays demonstrated that PEA-15 interfered with the ability of ERK2 to bind to nucleoporins. These results suggest that PEA-15 sequesters ERK2 in the cytoplasm at least in part by interfering with its ability to interact with nucleoporins, presenting a potential paradigm for regulation of ERK2 localization.

Active Transport, Cell Nucleus↗

PubMed1991

Digestion by pigs of non-starch polysaccharides in wheat and raw peas (Pisum sativum) fed in mixed diets.

The digestion by pigs of non-starch polysaccharides (NSP) in wheat and raw peas (Pisum sativum) fed in mixed diets was measured. In the four experimental diets, wheat was included at a constant 500 g/kg whilst peas contributed 0-300 g/kg and these were the only dietary sources of NSP. Separate estimates of digestibility for wheat and peas were obtained by using a multiple linear regression technique which also tested the possibility that the presence of peas might influence the digestibility of wheat NSP. There was little evidence of the latter and it was found that the digestibility of peas NSP (0.84) was considerably greater than that of wheat (0.65). The non-cellulosic polysaccharides (NCP) had twofold greater digestibilities than had cellulose for both foods with essentially all the peas NCP being digested. Faecal alpha, epsilon-diaminopimelic acid concentration increased with feeding of peas, suggesting stimulation of bacterial biomass production in the large intestine using the readily fermented peas NSP. All three major volatile fatty acids produced by large intestinal fermentation were detected in jugular blood and increased significantly with increasing peas inclusion rate in the diet.

Animal Feed↗

PubMed2000

Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism.

PEA-15 is a small, death effector-domain (DED)-containing protein that was recently demonstrated to inhibit tumor necrosis factor-alpha-induced apoptosis and to reverse the inhibition of integrin activation due to H-Ras. This led us to investigate the involvement of PEA-15 in Ras signaling. Surprisingly, PEA-15 activates the extracellular signal receptor-activated kinase (ERK) mitogen-activated protein kinase pathway in a Ras-dependent manner. PEA-15 expression in Chinese hamster ovary cells resulted in an increased mitogen-activated protein kinase kinase and ERK activity. Furthermore, PEA-15 expression leads to an increase in Ras guanosine 5'-triphosphate loading. PEA-15 bypasses the anchorage dependence of ERK activation. Finally, the effects of PEA-15 on integrin signaling are separate from those on ERK activation. Heretofore, all known DEDs functioned in the regulation of apoptosis. In contrast, the DED of PEA-15 is essential for its capacity to activate ERK. The ability of PEA-15 to simultaneously inhibit apoptosis and potentiate Ras-to-Erk signaling may be of importance for oncogenic processes.

3T3 Cells↗

PubMed1997

The influence of micronization, dehulling, and enzyme supplementation on the nutritional value of peas for laying hens.

Two experiments were conducted to determine the effects of micronization (infrared heat treatment), dehulling, or enzyme supplementation on the nutritive value of three cultivars (Impala, Radley, and Sirius) of peas in laying hens. In Experiment 1, 280 White Leghorn hens were fed diets containing micronized and dehulled peas for a period of 12 wk. The dietary inclusion of peas was 600 g/kg (correction was made for the amounts of hulls in those diets that contained dehulled peas). Egg production (P < or = 0.05), feed conversion (P > or = 0.05), and egg mass output (P < or = 0.05) were lower for birds fed untreated peas. Daily feed intake, egg weight, and albumen quality were not affected. Egg production, feed conversion, and egg mass output were similar for layers fed diets containing micronized peas and those fed the wheat-soybean control diet. Except for daily feed intake, which was reduced (P < or = 0.05), dehulling did not affect (P > or = 0.05) the feeding value of peas. The efficacy of dietary inclusion of a crude enzyme (pectinase) was evaluated in another experiment (8 wk). Pectinase was included in the experimental diets at 0, 50, and 100 U/kg and fed to 252 layers. The inclusion level of peas in these diets was 650 g/kg. There was no effect (P > or = 0.05) of enzyme supplementation on all production traits. Egg production, feed conversion, and egg mass output were 81.9, 83.6, and 83.0%; 1.61, 1.59, and 1.59 and 50.0, 51.2, and 50.3 at 0, 50, and 100 U/kg levels, respectively. It can be concluded that of the treatments tested only micronization had a positive effect on the feeding value of peas for laying hens.

Animal Feed↗

PubMed1983

Mechanism of the increase in cytochrome c oxidase activity in pea cotyledons during seed hydration. The presence of free cytochrome-c-oxidase subunits in dry cotyledons and their probable assembly into the holoenzyme during seed hydration.

The increase in cytochrome c oxidase activity in pea cotyledons during seed hydration was investigated with two kinds of antibodies against the enzymes purified from mitochondria of pea shoot and sweet potato root. The antibody against the pea enzyme recognized only the largest of the enzyme subunits (subunit I), while that against the sweet potato one did other three of the pea enzyme subunits: the second largest (subunit II) and the two smallest (subunits IV and V). There was no increase in the amount of protein immunoprecipitated with the anti-(pea enzyme) antibody in a crude fraction of cotyledon membranes during seed hydration, despite the marked increase in cytochrome c oxidase activity. Neither cycloheximide nor chloramphenicol had any effect on the activity or the amount. The crude membrane fraction from dry cotyledons contained an enzymatically inert protein precipitated with the anti-(pea enzyme) antibody. The inert protein could be separated from the active enzyme protein through solubilization of the protein from the membranes with various concentrations of Triton X-100. It consisted of only one kind of polypeptide with the same molecular weight as subunit I and decreased with the concomitant increase in the active enzyme protein during seed hydration. Dry pea cotyledons also contained a soluble protein that was immunoprecipitated by antibody to the sweet potato enzyme. The soluble form of the immunoreactive protein decreased with the concomitant increase in active cytochrome c oxidase protein in the crude membrane fraction from the cotyledons during seed hydration. None of these changes during seed hydration were inhibited by cycloheximide or chloramphenicol. The soluble, immunoreactive protein contained only one kind of polypeptide, of which the molecular weight was identical to that of subunit IV. The mitochondrial inner membranes of dry cotyledons were separated into three fractions by sucrose density gradient centrifugation. The lightest was the richest of the three in the enzymatically inert protein immunoprecipitated with the anti-(pea enzyme)antibody; cytochrome c oxidase activity in this fraction increased immediately after the onset of seed hydration. These results indicate that a membrane-bound, free form of subunit I and a soluble, free form of subunit IV of cytochrome c oxidase exist in dry pea cotyledons. We propose that these free forms of subunits are assembled with the other subunits to form the active cytochrome c oxidase during seed hydration.

Electron Transport Complex IV↗

PubMed1996

An implantable intracardiac accelerometer for monitoring myocardial contractility. The Multicenter PEA Study Group.

As the myocardium contracts isometrically, it generates vibrations that are transmitted throughout the heart. These vibrations can be measured with an implantable microaccelerometer located inside the tip of an otherwise conventional unipolar pacing lead. These vibrations are, in their audible component, responsible for the first heart sound. The aim of this study was to evaluate, in man, the clinical feasibility and reliability of intracavity sampling of Peak Endocardial Acceleration (PEA) of the first heart sound vibrations using an implantable tip mounted accelerometer. We used a unidirectional accelerometer located inside the stimulating tip of a standard unipolar pacing lead: the sensor has a frequency response of DC to 1 kHz and a sensitivity of 5 mV/G (G = 9.81 m/s-2). The lead was connected to an external signal amplifier with a frequency range of 0.05-1,000 Hz and to a peak-to-peak detector synchronized with the endocardial R wave scanning the isovolumetric contraction phase. Following standard electrophysiological studies, sensor equipped leads were temporarily inserted in the RV of 15 patients (68 +/- 15 years), with normal regional and global ventricular function, to record PEA at rest, during AAI pacing, during VVI pacing, and during dobutamine infusion (up to 20 micrograms/kg per min). PEA at baseline was 1.1 G +/- 0.5 (heart rate = 75 +/- 14 beats/min) and increased to 1.3 G +/- 0.9 (P = NS vs baseline) during AAI pacing (heart rate = 140 beats/min) and to 1.4 G +/- 0.5 (P = NS vs baseline) during VVI pacing (heart rate = 140 beats/min). Dobutamine infusion increased PEA to 3.7 G +/- 1.1 (P < 0.001 vs baseline), with a heart rate of 121 +/- 13 beats/min. In a subset of three patients, simultaneous hemodynamic RV monitoring was performed to obtain RV dP/dtmax, whose changes during dobutamine and pacing were linearly related to changes in PEA (r = 0.9; P < 0.001). In conclusion, the PEA recording can be consistently and safely obtained with an implantable device. Pharmacological inotropic stimulation, but not pacing induced chronotropic stimulation, increases PEA amplitude, in keeping with experimental studies, suggesting that PEA is an index of myocardial contractility. Acute variations in PEA are closely paralleled by changes in RV dP/dtmax, but are mainly determined by LV events. The clinical applicability of the method using RV endocardial leads and an implantable device offers potential for diagnostic applications in the long-term monitoring of myocardial function in man.

Acceleration↗

PubMed2004

Effect of field pea level on intake, digestion, microbial efficiency, ruminal fermentation, and in situ disappearance in beef steers fed forage-based diets.

Four ruminally and duodenally cannulated crossbred beef steers (397+/-55 kg initial BW) were used in a 4 x 4 Latin square to evaluate the effects of increasing level of field pea supplementation on intake, digestion, microbial efficiency, ruminal fermentation, and in situ disappearance in steers fed moderate-quality (8.0% CP, DM basis) grass hay. Basal diets, offered ad libitum twice daily, consisted of chopped (15.2-cm screen) grass hay. Supplements were 0, 0.81, 1.62, and 2.43 kg (DM basis) per steer daily of rolled field pea (23.4% CP, DM basis) offered in equal proportions twice daily. Steers were adapted to diets on d 1 to 9; on d 10 to 14, DMI were measured. Field pea and grass hay were incubated in situ, beginning on d 10, for 0, 2, 4, 8, 12, 16, 24, 36, 48, 72, and 96 h. Ruminal fluid was collected and pH recorded at -2, 0, 2, 4, 6, 8, 10, and 12 h after feeding on d 13. Duodenal samples were taken for three consecutive days beginning on d 10 in a manner that allowed for a collection to take place every other hour over a 24-h period. Linear, quadratic, and cubic contrasts were used to evaluate the effects of increasing field pea level. Total DMI and OMI increased quadratically (P = 0.09), whereas forage DMI decreased quadratically (P = 0.09) with increasing field pea supplementation. There was a cubic effect (P < 0.001) for ruminal pH. Ruminal (P = 0.02) and apparent total-tract (P = 0.09) NDF disappearance decreased linearly with increasing field pea supplementation. Total ruminal VFA concentrations responded cubically (P = 0.008). Bacterial N flow (P = 0.002) and true ruminal N disappearance (P = 0.003) increased linearly, and apparent total-tract N disappearance increased quadratically (P = 0.09) with increasing field pea supplementation. No treatment effects were observed for ruminal DM fill (P = 0.82), true ruminal OM disappearance (P = 0.38), apparent intestinal OM digestion (P = 0.50), ruminal ADF disappearance (P = 0.17), apparent total-tract ADF disappearance (P = 0.35), or in situ DM disappearance of forage (P = 0.33). Because of effects on forage intake and ruminal pH, field peas seem to act like cereal grain supplements when used as supplements for forage-based diets. Supplementing field peas seems to effectively increase OM and N intakes of moderate-quality grass hay diets.

Animal Feed↗

PubMed2000

Effects of pea, barley, and alfalfa silage on ruminal nutrient degradability and performance of dairy cows.

Six Holstein cows in early lactation were used in a double 3 x 3 Latin square design to determine the effects of feeding diets with pea silage, relative to barley silage, or alfalfa silage. Cows were fed rations formulated to contain 50:50 forage:concentrate ratio. Two ruminally fistulated cows were used in a randomized complete block design to determine ruminal nutrient degradability for pea silage relative to barley and alfalfa silages. Pea silage contained lower neutral detergent fiber (NDF), acid detergent fiber, and starch concentrations but higher crude protein than barley silage. Compared with alfalfa silage, pea silage had higher starch and NDF but lower crude protein content. Pea and alfalfa silage had similar effective ruminal degradability of dry matter, which was higher than that of barley silage. The rate of degradation and effective ruminal degradability of NDF was highest for alfalfa silage, intermediate for pea silage and lowest for barley silage. Results of the lactation trial showed that dry matter intake and milk yield were not affected by forage source. Milk composition was similar for cows fed pea or barley silage; however, cows fed pea silage produced milk with a higher fat and a lower protein percentage than those fed the alfalfa silage. Pea silage can replace barley or alfalfa silage as a forage source for dairy cows in early lactation.

Animal Nutritional Physiological Phenomena↗