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PubMed2005

Microsatellite markers for powdery mildew resistance in pea (Pisum sativum L.).

Powdery mildew is a common disease of field pea, Pisum sativum L., and is caused by the ascomycete fungus Erysiphe pisi. It can cause severe damage in areas where pea is cultivated. Today breeders want to develop new pea lines that are resistant to the disease. To make the breeding process more efficient, it is desirable to find genetic markers for use in a marker-assisted selection (MAS) strategy. In this study, microsatellites (SSR) were used to find markers linked to powdery mildew resistance. The resistant pea cultivar '955180' and the susceptible pea cultivar 'Majoret' were crossed and F2 plants were screened with SSR markers, using bulked segregant analysis. A total of 315 SSR markers were screened out of which five showed linkage to the powdery mildew resistance gene. No single marker was considered optimal for inclusion in a MAS program. Instead, two of the markers can be used in combination, which would result in only 1.6% incorrectly identified plants. Thus SSR markers can be successfully used in marker-assisted selection for powdery mildew resistance breeding in pea.

Ascomycota↗

PubMed1996

Red light-induced appearance of phosphotyrosine-like epitopes on nuclear proteins from pea (Pisum sativum L.) plumules.

As assayed by western blot analysis, red light induces the appearance of epitopes recognized by anti-phosphotyrosine antibodies in several pea nuclear proteins. The immunostaining is blocked by preadsorbing the antibodies with phosphotyrosine but not by preadsorbing them with phosphoserine or phosphothreonine. This light response is observed whether the red light irradiation is given to pea plumules or nuclei isolated from the plumules. The red-light-induced response seen in plumules is reversible by a subsequent far-red-light irradiation, indicating that the likely photoreceptor for this response may be phytochrome. By immunoblot analysis pea phytochrome A, but not phytochrome B, can be detected in proteins extracted from pea nuclear chromatin-matrix preparations. Phytochrome A and the protein bands immunostained by anti-phosphotyrosine antibodies can be solubilized from unirradiated pea chromatin by 0.3 M NaCl, but irradiating this preparation with red light does not induce the appearance of phosphotyrosine-like epitopes in any nuclear proteins. These results suggest that the association of phytochrome with purified pea nuclei is such that its conversion to the far-red light-absorbing form can induce a post-translational epitope change in nuclear proteins in vivo.

Epitopes↗

PubMed1980

Effect of moderately acidic pH on heat resistance of Clostridium sporogenes spores in phosphate buffer and in buffered pea puree.

The effect of pH in the range 5.0 to 7.0 on the thermal destruction of spores of Clostridium sporogenes putrefactive anaerobe 3679 was examined by three methods: a capillary tube method in which spores were suspended in phosphate buffers, a thermoresistometer method in which spores were suspended in buffered pea puree adjusted to the same set of pH values, and a thermal death time can method in which spores were again suspended in buffered pea puree. The results indicated that increasing acidity is, in general, accompanied by decreasing heat resistance, although the pH effect was more pronounced at the higher than at the lower processing temperatures. Certain pH values appear to be critical, as they produced, in all three sets of experiments, effects which would not be predicted by the overall relationship between acidity and spore heat resistance. Differences between heat resistance in phosphate buffer as compared with that in pea puree adjusted to the same pH were also noted. D-values in buffer were found to be lower than those in pea puree, except at the highest temperatures coupled with the lowest pH values. The differences between buffer D-value and pea puree D-value were found to increase with increasing pH and with decreasing temperature. On the other hand, at all pH values examined, z-values determined in buffer were somewhat higher than those determined in pea puree adjusted to the same pH.

Buffers↗

PubMed1988

Localization of replication origins in pea chloroplast DNA.

The locations of the two replication origins in pea chloroplast DNA (ctDNA) have been mapped by electron microscopic analysis of restriction digests of supercoiled ctDNA cross-linked with trioxalen. Both origins of replication, identified as displacement loops (D-loops), were present in the 44-kilobase-pair (kbp) SalI A fragment. The first D-loop was located at 9.0 kbp from the closest SalI restriction site. The average size of this D-loop was about 0.7 kbp. The second D-loop started 14.2 kbp in from the same restriction site and ended at about 15.5 kbp, giving it a size of about 1.3 kbp. The orientation of these two D-loops on the restriction map of pea ctDNA was determined by analyzing SmaI, PstI, and SalI-SmaI restriction digests of pea ctDNA. One D-loop has been mapped in the spacer region between the 16S and 23S rRNA genes. The second D-loop was located downstream of the 23S rRNA gene. Denaturation mapping of recombinants pCP 12-7 and pCB 1-12, which contain both D-loops, confirmed the location of the D-loops in the restriction map of pea ctDNA. Denaturation-mapping studies also showed that the two D-loops had different base compositions; the one closest to a SalI restriction site denatured readily compared with the other D-loop. The recombinants pCP 12-7 and pCB 1-12 were found to be highly active in DNA synthesis when used as templates in a partially purified replication system from pea chloroplasts. Analysis of in vitro-synthesized DNA with either of these recombinants showed that full-length template DNA was synthesized. Recombinants from other regions of the pea chloroplast genome showed no significant DNA synthesis activity in vitro.

Chloroplasts↗

PubMed1995

Response of the calf pancreas to differently processed soya bean and pea diets.

The purpose of this study was to determine the effect of replacing skim-milk powder by differently treated soya bean or pea products on growth, pancreas size and pancreatic enzyme activities in calves. Three separate experiments have been performed. In experiments 1 and 2, 28 and 21 male Holstein calves were divided into 4 or 3 groups, respectively, and fed either dairy products or milk substitutes in which protein was mainly provided by soya bean products differing in their protein concentration due to the technological processing applied. In experiment 3, 45 male Holstein calves were divided into 3 groups and were fed either dairy products, or raw or flaked pea flour as a protein source. After an experimental period of 99 +/- 4 days in experiments 1 and 2, and of 88 days in experiment 3, animal growth rate was significantly lower with raw pea flour (16%) and with the soya bean diet, which was highly concentrated in carbohydrates and allergenic proteins (13-27%). Pancreas weight decreased significantly (16-18%) with pea diets and tended to be lower (NS) with the water extracted, concentrated and heated flour (soya bean). Amylase-specific activity increased significantly (43%) with pea diets but showed opposite tendencies with the most refined soya bean products. Proteolytic enzyme activities were slightly influenced by dietary protein source, but this was not as obvious as in the literature reviewed. Specific messenger RNAs corresponding to amylase, trypsin and chymotrypsin seemed to increase (NS) with the soya bean diets, particularly with the less elaborated one. However, further investigations are required before any conclusions may be drawn concerning regulation levels of pancreatic adaptation to dietary protein. According to this study and the literature, results concerning pancreatic response to diets were different suggesting that the origin of soya bean, pea seeds and technological treatments applied to them were of great importance. Also, the level of incorporation into milk substitute and the presence of more or less antinutritional factors could influence pancreatic enzyme variations by complex mechanisms.

Amylases↗

PubMed1996

Sustained antidepressant effect of PEA replacement.

Phenylethylamine (PEA), an endogenous neuroamine, increases attention and activity in animals and has been shown to relieve depression in 60% of depressed patients. It has been proposed that PEA deficit may be the cause of a common form of depressive illness. Fourteen patients with major depressive episodes that responded to PEA treatment (10-60 mg orally per day, with 10 mg/day selegiline to prevent rapid PEA destruction) were reexamined 20 to 50 weeks later. The antidepressant response had been maintained in 12 patients. Effective dosage did not change with time. There were no apparent side effects. PEA produces sustained relief of depression in a significant number of patients, including some unresponsive to the standard treatments. PEA improves mood as rapidly as amphetamine but does not produce tolerance.

Adult↗

PubMed2006

Phosphorus fractions in manure from growing pigs receiving diets containing micronized peas and supplemental enzymes.

Different livestock feeds manipulations have been reported to reduce the total P concentration in manure. Information on the influence of these dietary manipulation strategies on the forms of P in manure is, however, limited. This study was, therefore, conducted to investigate the effect of diet manipulation through feed micronization and enzyme supplementation on the forms of P in swine manure. Eight growing pigs were fed four diets: barley-raw pea (BRP), barley-micronized pea (BMP), barley-raw pea with enzyme (BRPE), and barley-micronized pea with enzyme (BMPE) in a 4 x 4 Latin square design. Because we are interested in the effect of enzyme cocktail and pea micronization on manure P, we did not reduce the non-phytate P with enzyme addition in this study. The fecal material and urine were collected and analyzed for total P. Fecal material was fractionated to determine the total P in H2O-, NaHCO3-, NaOH-, and HCl-extractable fractions. The total P in the residual fractions was also determined. About 98% of the total P excreted by the pigs was found in the fecal material. Inclusion of micronized pea in pig diet did not have any significant effect (p > 0.1) on either the total P or the different P fractions in the manure. The labile P (the sum of H2O-P and NaHCO3-P) was significantly reduced (p < 0.05) by the addition of enzyme to swine diets. Pigs fed the BRPE and BMPE had 14 and 18% lower labile P, respectively, compared with pigs fed the BRP. Enzyme addition to pig diets reduced not only the total P in manure, but also the labile P fraction, which is of great environmental concern. Thus, the potential of P loss to runoff and the subsequent eutrophication can be reduced by enzyme addition to pig diets.

Animal Feed↗

PubMed2003

[Graviresponse in higher plants and its regulation in molecular bases: relevance to growth and development, and auxin polar transport in etiolated pea seedlings].

We review the graviresponse under true and simulated microgravity conditions on a clinostat in higher plants, and its regulation in molecular bases, especially on the aspect of auxin polar transport in etiolated pea (Pisum sativum L. cv. Alaska) seedlings which were the plant materials subjected to STS-95 space experiments. True and simulated microgravity conditions substantially affected growth and development in etiolated pea seedlings, especially the direction of growth of stems and roots, resulting in automorphosis. In etiolated pea seedlings grown in space, epicotyls were the most oriented toward the direction far from the cotyledons, and roots grew toward the aerial space of Plant Growth Chamber. Automorphosis observed in space were well simulated by a clinorotation on a 3-dimensional clinostat and also phenocopied by the application of auxin polar transport inhibitors of 2,3,5-triiodobenzoic acid, N-(1-naphtyl)phthalamic acid and 9-hydroxyfluorene-9-carboxylic acid. Judging from the results described above together with the fact that activities of auxin polar transport in epicotyls of etiolated pea seedlings grown in space substantially were reduced, auxin polar transport seems to be closely related to automorphosis. Strenuous efforts to learn in molecular levels how gravity contributes to the auxin polar transport in etiolated pea epicotyls resulted in successful identification of PsPIN2 and PsAUX1 genes located in plasma membrane which products are considered to be putative efflux and influx carriers of auxin, respectively. Based on the results of expression of PsPIN2 and PsAUX1 genes under various gravistimulations, a possible role of PsPIN2 and PsAUX1 genes for auxin polar transport in etiolated pea seedlings will be discussed.

Biological Transport↗

PubMed2004

Effect of field pea-based creep feed on intake, digestibility, ruminal fermentation, and performance by nursing calves grazing native range in western North Dakota.

Two experiments evaluated digestive and performance effects of field pea-based creep feed in nursing calf diets. In Exp.1, eight nursing steer calves (145 +/- 27 kg initial BW) with ruminal cannulas were used to evaluate effects of supplementation and advancing season on dietary composition, intake, digestion, and ruminal fermentation characteristics. Treatments were unsupplemented control (CON) and field pea-based creep (SUP; 19.1% CP, DM basis) fed at 0.45% BW (DM basis) daily. Calves grazed native range with their dams from early July through early November. Periods were 24 d long and occurred in July (JUL), August (AUG), September (SEP), and October (OCT). Experiment 2 used 80 crossbred nursing calves, 48 calves in yr 1 and 32 calves in yr 2 (yr 1 = 144 +/- 24 kg; yr 2 = 121 +/- 20 kg initial BW), to evaluate effects of field pea-based creep on calf performance. Treatments included unsupplemented control (CON); field pea-based creep feeds containing either 8% (LS); or 16% (HS) salt; and soybean meal/field pea-based creep containing (as-fed basis) 16% salt (HIPRO). Masticate samples from SUP calves in Exp.1 had greater CP (P = 0.05) than those from CON calves. Forage CP and ADIN decreased linearly with advancing season (P = 0.01 and 0.03, respectively). In vitro OM digestibility of diet masticate decreased from JUL to OCT (P < 0.01; 58.5 to 41.3%). Forage intake did not differ (P = 0.33) between treatments but increased linearly with advancing season (1.67, 1.90, 3.12, 3.38 kg/d for JUL, AUG, SEP, and OCT, respectively; P < 0.01). Milk intake (percentage of BW) did not differ (P = 0.56) between CON and SUP calves but decreased linearly (P < 0.01) with advancing season. Supplemented calves had greater (P = 0.03) total intake (g/kg of BW; forage + milk + creep) compared with CON calves. Treatment did not affect (P < 0.30) rate of in situ disappearance of forage or creep. Forage DM, CP, and creep DM disappearance rate decreased linearly (P < or = 0.02) with advancing season. Supplementation decreased (P = 0.05) ruminal pH, whereas ruminal ammonia and VFA concentrations were greater (P < or = 0.02) in SUP calves. In Exp. 2, creep-fed calves had greater ADG and final BW than CON calves (P < 0.01). Calves offered HS tended (P = 0.07) to have increased gain efficiency above CON than LS calves. Field peas can be used as an ingredient in creep feed to increase calf weight gain without negatively affecting ruminal fermentation and digestion.

Animal Feed↗

PubMed2002

Forage intake, meal patterns, and milk production of lactating dairy cows fed grass silage or pea-wheat bi-crop silages.

This study investigated the feed intake, milk production, and plasma nutrient status in dairy cows fed inter-cropped pea-wheat (bi-crop) silages comprised of contrasting ratios of pea to wheat. Spring peas (cv. Magnus) and wheat (cv. Axona) sown at either high (75:25) or low (25:75) pea inclusion rates were harvested after 13 (Cut 1) or 15 (Cut 2) wk. Eighteen Holstein-Friesian cows between wk 9 and 10 of lactation were used in a cyclical changeover design with three 28-d periods. Cows were fed the bi-crop silages and 6 kg of concentrates or second-cut grass silage supplemented with 6 (GS6) or 9 (GS9) kg/d of concentrates. Forage intakes were higher when bi-crops were fed (10.3 to 11.4 kg dry matter [DM]/d) than when grass silage was fed (8.6 kg DM/d). Total DM intake was similar among cows fed the bi-crop silages and GS9 diets, but intakes for GS6 were at least 1.7 kg DM/d lower. Increasing the pea inclusion rate increased the crude protein (CP) content of the ration, but it did not enhance forage quality or animal performance. The rate of intake of the different forages was similar, so that the higher intakes of bi-crop silages were associated with more time spent at the feedbunk and an increased number of meals. Diet digestibility ranged from 531 to 650 g/kg, and the highest value was given by the Cut 1 bi-crop silage diet. Milk yield tended to be similar for cows fed the Cut 2 bi-crop and GS9 diets, and these values were at least 1.7 kg higher than those for cows fed on other treatments. Generally, the bi-crop diets resulted in higher milk fat contents and lower polyunsaturated fatty acid contents. Milk protein content was highest for cows fed the GS9 diet. Blood metabolite content was unaffected by treatment except for blood urea nitrogen content, which was higher in cows fed the bi-crop silages, reflecting reduced N-use efficiency with these diets. The study showed that pea-wheat bi-crop silages can be used to replace moderate-quality grass silage in dairy cow rations, but their role as alternatives to high-quality forages requires additional investigation.

Animal Nutritional Physiological Phenomena↗

PubMed1992

Effects of raw pea flour on nutrient digestibility and immune responses in the preruminant calf.

Two milk substitute diets for which the protein was provided either exclusively by skim milk powder (control) or partially (34%) by dehulled raw pea flour were given for 2 and 4 wk, respectively, to five preruminant calves, each fitted with a reentrant ileocecal cannula. Ileal apparent digestibility was lower with the pea diet during wk 1 than with the control diet. Four of the cannulated calves exhibited significant intolerance to the pea diet, resulting in lower digestibility during wk 4. In contrast, fecal digestibility of the pea diet, measured in four additional calves without reentrant cannulas, did not significantly decrease between wk 1 and 4. The AA composition of ileal digesta from the first group of calves did not vary greatly, suggesting that the differences observed in their apparent digestibility of proteins were due mainly to changes in the loss of endogenous proteins. However, pea legumin survived digestion in the small intestine in amounts generally equivalent to 1 to 3% of intake. Most of that undigested fraction was smaller than the native legumin: 40 to 200 kDa instead of 360 kDa. Also, a 45-kDa fragment was detected in the urine. Increased intestinal permeability could have favored the development of the high systemic anti-pea antibody titers that were observed in all of the calves.

Amino Acids↗

PubMed2001

Transforming growth factor-beta induced collagenase-3 production in human osteoarthritic chondrocytes is triggered by Smad proteins: cooperation between activator protein-1 and PEA-3 binding sites.

OBJECTIVE: To examine the signaling pathways leading to transforming growth factor-beta (TGF-beta) induced collagenase-3 production in human osteoarthritic (OA) chondrocytes, as well as the transcription factors and their binding sites involved in the transcriptional control of collagenase-3 gene. METHODS: Identification of the TGF-beta signaling pathway was by Western immunoblotting using specific antibodies for the phosphorylated forms of p44/42 and p38 MAPK, SAPK/JNK, and the Smad2 protein. Electromobility shift assays (EMSA) were carried out for activator protein- (AP-1), polyomavirus enhancer A (PEA-3), activin-response-element-like, Smad-binding-element-like, and TGF-beta inhibitory element oligonucleotides. Supershift assays using antibodies to the Jun, Fos, and Smad families of proteins were used for identification of transcription factors. Chondrocyte transfections were also performed using the -133CAT collagenase-3 promoter plasmid (containing PEA-3, AP-1, and TATA sites) and mutated AP-1 and PEA-3 sites. RESULTS: The primary target of TGF-beta induced collagenase-3 in OA chondrocytes was the Smad2 protein, with significant phosphorylation within 5 min. Contrasting with the Smad2, the untreated OA chondrocytes already had detectable levels of the phosphorylated forms of p38 and p44/42 MAPK. Of the oligonucleotides tested, EMSA revealed that TGF-beta treated OA chondrocyte proteins bound only to the AP-1 and PEA-3. Supershifts with the AP-1 oligonucleotide showed the presence of the Jun (c-Jun, JunB, JunD) and Fos (c-Fos, FosB, Fra-1, Fra-2) proteins in the untreated and TGF-beta treated OA chondrocytes, whereas only Smad proteins (Smad2, 3, 4) were present in the AP-1 binding proteins from the TGF-beta treated chondrocytes. The AP-1 mutation decreased both basal (95%) and TGF-beta induced (99%) collagenase-3 production, whereas the PEA-3 mutation decreased the basal (15%) but more significantly (50%) the TGF-beta induced transcription. CONCLUSION: Smad proteins are the main cytoplasmic signaling pathways in TGF-beta stimulated collagenase-3 in OA chondrocytes. The AP-1 site appears critical for upregulation of collagenase-3 production, but TGF-beta stimulation requires both AP-1 and PEA-3 sites for optimal response.

Aged↗

PubMed2003

Assessment of residual immunoreactivity in red or white wines clarified with pea or lupin extracts.

Vegetable proteins could be a suitable alternative to animal proteins in the clarification of wine, but their residues could represent a risk for subjects with food allergy or intolerance. The aim of this study was to investigate the presence of specific immunoreactivity in red and white wines treated, as must or wine, with vegetable proteins in the clarification process. The proteins considered were prepared from lupins and peas, which are not included among the allergens listed in annex Illbis of Directive 2003/89/EC. The presence of residual immunoreactivity to specific rabbit anti-lupin and anti-pea polyclonal antibodies in treated wines was assessed by electrophoresis (SDS-PAGE) and immunoblotting. Residual protein was not detectable in red wines clarified with lupin, pea or a mixture of pea and lupin proteins or in white wines clarified with pea proteins. A small number of musts treated with lupin or pea proteins and white wines treated with lupin proteins yielded equivocal results, probably because of the presence of interfering material (e.g., sugar-rich proteins from grape and yeast). The use of bentonite as a secondary clarifying agent is therefore recommended since its combination with vegetable proteins is particularly effective in removing overall protein immunoreactivity.

Animals↗

PubMed2003

[Tendril inheritance in semi-leafless pea and its utilization in breeding].

Using semi-leafless pea and common pea, the authors studied tendril character, its inheritance law and how to use it in pea breeding. The results were as follows: Semi-leafless pea had well developed tendrils; They twined with each other and formed an arbor structure. This ideal structure had greatly increased lodging resistance capability,improved canopy's air and light level, and remarkably increased new varieties yield. So, semi-leafless pea was one of the most important materials in lodging resistance breeding. Tendril gene, af, and seed color gene i, in semi-leafless pea was linked on chromosome I, and cross-over value was 5.72%.

English Abstract↗

PubMed2005

[Effects of low temperature at 10 degrees C on some antioxidant enzyme activities and ultrastructures of hypocotylar cells in mung bean and garden pea].

Mung bean (Phaseolus radiatus Linn.) and garden pea (Pisum satium Linn.), which were stressed 4 days under a low temperature of 10 degrees C, were used as materials to study the cold tolerance of plant with different resistance. On the 2nd and 3rd day under 10 degrees C stress, both the malondialdehyde (MDA) content and the superoxide dismutase (SOD), catalase (CAT) and peroxidase (POD) activities increased significantly in hypocotylar cells of mung bean, so did SOD activity in garden pea, but other physiological indexes in garden pea were not different from the non-treatment groups (Figs. 1-5). In hypocotylar cells of mung bean, SOD activity always maintain at the highest level in a period of time,and so does POD activity (Figs. 3, 4). Ultrastructural results after stress indicated as follows: (1) Plastids in hypocotylar cells of mung bean accumulated much starch (Plate I-6), whereas the form of plastids in hypocotylar cells of garden pea changed maskedly to become dumb-bell-shaped, round or irregular, with the last one being the most common form (Plate I-8, 12); (2) In both mung bean and garden pea, central vacuole was divided into small vacuoles (Plate I-4, 10), and the number of mitochondria increased and became aggregated (Plate I-3, 11, 12). Judging from the activities of protective enzymes and ultrastructures, 10 degrees C low temperature caused non-lethal, temporary injuries to hypocotyls ultrastructures in mung bean, but no visible injury at all, and even improved its cold tolerance to a certain degree in garden pea.

Catalase↗

PubMed2005

First report of occurrence of two viruses on pea field in Iran.

An intensive survey was conducted to identify virus diseases affecting pea crops in Tehran province of Iran. A total of 270 pea samples were collected randomly from pea fields. samples were tested by Double Antibody Sandwich Enzyme Linked Immunosorbent Assay (DAS-ELISA) using polyclonal antisera prepared against PSBMV (AS-0129, DSMZ, Braunschweig, Germany) and TSWV (AS-0580, DSMZ, Braunschweig, Germany). Virus disease incidence in pea samples was followed by PSBMV (33%) TSWV (24.4%) and PSBMV+TSWV (17.77). The positive samples with PSBMV were extracted in 0.05M phosphate buffer pH 6.5-7 containing 2% pvp and inoculated on Pisum sativum, Vicia faba, Chenopodium quinoa, Chenopodium amaranticolor. That produced in Pisum sativum; leaflets roll downwards, shoots curl, internodes shorten and plants are rosetted. Early infections reduce flower and fruit formation or eliminate their development. Broad bean has symptoms accompanied by a certain margin rolling and leaflet distortion. In Chenopodium amaranticolor necrotic local lesions and Chenopodium quinoa chlorotic local lesions had produced. The positive samples with TSWV were extracted in 0.01 M phosphate buffer containing 1% Na2 SO3 and inoculated on Petunia hybrida, Pisum sativum. TSWV causes several symptoms in infected peas, including brown leaf petiole and stem coloration, leaflet spotting, vein necrosis. In petunia hybrida after approximately 5 days showed local necrotic lesion. Biological purification in TSWV with chlorotic local lesions in Petunia hybrida and in PSBMV; chlorotic local lesions in Chenopodium quinoa were done. In PSBMV, back inoculated on Pisum sativum and Vicia faba also tested with DAS-ELISA. RT-PCR confirmed the results. This is the first report of PSBMV and TSWV naturally infecting pea in Iran.

Enzyme-Linked Immunosorbent Assay↗

PubMed1989

[Digestion of pea and soya proteins in the preruminant calf. I. Circulating levels of nutrients, antibody formation and intestinal permeability to macromolecules].

Three milk-substitutes (control, pea and soya-bean)were given to 6 preruminant calves. In the control diet protein was almost entirely provided by skim milk powder. In the pea diet a pregelatinized dehulled pea flour provided 33.5% of the protein, the remainder being supplied by skim milk powder. In the soya-bean diet, 73.2% of the protein were provided by a soya-bean isolate and the remainder by whey powder. The concentrations of plasma triglycerides and the free alpha-amino nitrogen in the peripheral blood were lower with the pea and soya-bean diets than with the control diet before the morning meal, but became higher after feeding. That suggested a faster abomasal emptying of fat and protein with the pea and especially the soya-bean diet. Systemic antibody responses were induced against pea protein but not against soya-bean protein. No effect of the diet on the plasma concentration of immunoreactive beta-lactoglobulin was apparent after 6 days, suggesting there was no important change in gut permeability at least at that time.

Animals↗

PubMed1980

Mouse lymphoma cell lines resistant to pea lectin are defective in fucose metabolism.

Two mutants of the BW5147 mouse lymphoma cell line have been selected for their resistance to the toxic effects of pea lectin. These cell lines, termed PLR1.3 and PHAR1.8 PLR7.2, have a decreased number of high affinity pea lectin-binding sites (Trowbridge, I.S., Hyman, R., Ferson, T., and Mazauskas, C. (1978) Eur. J. Immunol. 8, 716-723). Intact cell labeling experiments using [2-3H]mannose indicated that PLR1.3 cells have a block in the conversion of GDP-[3H]mannose to GDP-[3H]fucose whereas PHAR1.8 PLR7.2 cells appear to be blocked in the transfer of fucose from GDP-[3H]fucose to glycoprotein acceptors. In vitro experiments with extracts of PLR1.3 cells confirmed the failure to convert GDP-mannose to GDP-fucose and indicated that the defect is in GDP-mannose 4,6-dehydratase (EC 4.2.1.47), the first enzyme in the conversion of GDP-mannose to GDP-fucose. The block in the PLR1.3 cells could be bypassed by growing the cells in the presence of fucose, demonstrating that an alternate pathway for the production of GDP-fucose presumably via fucose 1-phosphate is functional in this line. PLR1.3 cells grown in 10 mM fucose showed normal high affinity pea lectin binding. PHRA1.8 PLR7.2 cells synthesize GDP-fucose and have normal or increased levels of GDP-fucose:glycoprotein fucosyltransferase when assayed in vitro. The fucosyltransferases of this clone can utilize its own glycoproteins as fucose acceptors in in vitro assays. These findings indicate that this cell line fails to carry out the fucosyltransferase reaction in vivo despite the fact that it possesses the appropriate nucleotide sugar, glycoprotein acceptors, and fucosyltransferase. The finding of decreased glycoprotein fucose in two independent isolates of pea lectin-resistant cell lines and the restoration of high affinity pea lectin binding to PLR1.3 cells following fucose feeding strongly implicates fucose as a major determinant of pea lectin binding.

Animals↗