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PubMed1993

Effects of N-terminal truncations upon chloroplast NADP-malate dehydrogenases from pea and spinach.

Using the purification procedure of Fickenscher and Scheibe (Biochim. Biophys. Acta 749 (1983), 249-254) and a modification of the method, we produced a series of NADP-MDH forms from spinach and pea-leaf extracts that were characterized by a stepwise shortening of the N-terminal sequences. Limited proteolysis of the enzymes resulted in the generation of even shorter forms. Immunoprecipitation of the NADP-MDH from crude extracts revealed that the sequences of the intact enzymes from pea, spinach and maize started at a position (Ser) identical with that established for the Sorghum enzyme (Crétin, C., et al. (1990) Eur. J. Biochem. 192, 299-303). Spinach NADP-MDH isolated by conventional methods was shown to represent the intact form. Thus, the kinetic, regulatory and structural properties of the various truncated forms could be compared with those of an intact form. Removal of 5 or 11 amino acids, as occurred during isolation of the pea NADP-MDH, was without any significant effect. The enzymes were all dimeric and still exhibited the characteristic redox-regulatory properties. However, removal of 31 and 37 amino acids using aminopeptidase K resulted in the formation of active monomers characterized by only slightly lowered affinities towards the substrates, a shift of their pH optimum from 8 to 7, the loss of oxaloacetate inhibition and an increased maximal velocity. Although these forms lacked most or all of the N-terminal extra-peptide, including the 2 cysteines involved in redox-modification, they were still sensitive to the redox-potential. However, the low concentration of thiol required for immediate and complete restoration of any lost activity (40 mM beta-mercaptoethanol) suggested that this reaction might not be relevant for redox-regulation in vivo.

Amino Acid Sequence↗

PubMed1993

Differential regulation of S-adenosylmethionine synthetase isozymes by gibberellic acid in dwarf pea epicotyls.

Dwarf pea epicotyls contained a single activity peak of S-adenosylmethionine (AdoMet) synthetase (isozyme I). Gibberellic acid (GA3, 1 microM) induced two additional isozymes (II and III). Cycloheximide (20 microgram/ml) blocked the appearance of GA3-induced isozymes, suggesting that it is dependent on de novo protein synthesis. Conclusive proof was obtained by labelling the isozymes II and III with [35S]SO2-(4) in vivo. The purified 35S-labelled AdoMet synthetase isozymes (II, III) showed a single protein band that coincided with the single radioactive peak on SDS-PAGE. Molecular-sieve chromatography of the isozyme I from control dwarf pea epicotyls and three isozymes of GA3-treated epicotyls on Sepharose CL-6B showed a single activity peak with an identical molecular mass of 174 kDa for each isozyme. Analysis of purified AdoMet synthetase isozymes (I, II, III) on SDS-PAGE showed a single silver-stained protein band with a molecular mass of 87 kDa. This proved the dimeric nature of all the isozymes of AdoMet synthetase which could be physically separated by ion-exchange chromatography on DE-52. In vitro molecular hybridization of physically separated isozymes by NaCl-freeze-thaw treatment method revealed that the three isozymes (I, II, III) in GA3-treated dwarf pea epicotyls are formed through the random dimerization of two different species of enzyme subunits that differ in their net charge. Thus, the two flanking activity peaks (isozymes I, III) represent homodimers, while the middle activity peak (isozyme II) is a heterodimer. Apparently, the single isozyme I in control epicotyls is a product of one gene of AdoMet synthetase (SAM 1), while three isozymes in GA3-treated epicotyls are the product of two genes of AdoMet synthetase. We speculate that the differential regulation of AdoMet synthetase in GA3-treated epicotyls is achieved by the expression of an alternate gene of AdoMet synthetase (SAM 2).

Chromatography, Gel↗

PubMed1993

Metabolism and excretion of dimethoate following ingestion of overtolerance peas and a bolus dose.

Data to guide an exposure assessment were obtained by giving sugar peas containing overtolerance dimethoate residues (17 ppm; 8% oxon) and a bolus dose of dimethoate to a healthy adult male. The dimethoate tolerance on peas was and remains 2 ppm. Serial total urine samples were collected and analysed for dimethoate and its oxon, dimethylphosphate, dimethylphosphorothioate (DMTP) and dimethylphosphorodithioate. The dose of dimethoate administered was approx. 0.1 mg/kg body weight and produced no symptoms of toxicity. Dimethylphosphates appeared in the urine within 2 hr. The major metabolite (about 60%) was DMTP. Only traces (< 0.5%) of dimethoate and oxon were recovered from urine. Acetylcholinesterase inhibition was not observed although urinary metabolites were prominent, indicating that they are better indicators of acute exposure than cholinesterase inhibition. The results obtained using a bolus dose were virtually identical to those from the trial with overtolerance peas, and indicated that dimethoate is readily absorbed and its urinary metabolites are readily eliminated following exposures to low doses (0.1 mg/kg body weight).

Administration, Oral↗

PubMed1981

Clone banks of the mung bean, pea and spinach chloroplast genomes.

All but one of the PstI restriction fragments from mung bean, pea, and spinach chloroplast DNAs have been stably cloned into pBR322. Large fragments (15-54 kb) were cloned at low efficiencies which decreased with increasing fragment length. However, plasmids containing fragments above 25-30 kb were too unstable to be useful. In particular, pBR322 derivatives containing the largest mung bean and spinach fragments (34 kb and 54 kb, respectively) are extremely unstable and rapidly delete parts of the plasmid sequence. The PstI fragments of mung bean chloroplast DNA which cover the 34-kb PstI fragment have been cloned into pACYC177. After a search of several thousand recombinants we were unable to recover a clone containing a 12.2-kb pea chloroplast PstI fragment and suggest that some property of its sequence may be inimical to the cloning process. The identity of the cloned fragments to native chloroplast DNA restriction fragments is demonstrated by restriction analysis and the ability to construct detailed restriction maps of the mung bean and pea chloroplast genomes.

Base Sequence↗

PubMed1994

Cloning and characterization of the PDA6-1 gene encoding a fungal cytochrome P-450 which detoxifies the phytoalexin pisatin from garden pea.

The ability to detoxify pisatin, a phytoalexin produced by garden pea (Pisum sativum), is controlled by a family of PDA (pisatin demethylating ability) genes in the phytopathogenic fungus Nectria haematococa, MP (mating population) VI. Six known PDA genes each encode characteristic levels of inducible enzyme activity and are associated with different degrees of virulence on pea. To elucidate the phenotypic differences associated with these genes, we have cloned and characterized the PDA6-1 gene which encodes a pisatin-detoxifying enzyme and we compare it to another PDA gene, PDAT9. Pisatin demethylation was measured in PDA6-1 transformants of Aspergillus nidulans and shown to be regulated by glucose. The deduced amino acid (aa) sequence of PDA6-1 was 90% identical to that of the cytochrome P-450 encoded by PDAT9, but lacked nine aa at the C terminus, which has been postulated to be a site involved in substrate binding. A 35-bp sequence present upstream of a third PDA gene, PDA1, which appears to be important for induction of PDA1 by pisatin, was conserved in PDAT9, but not in PDA6-1. We conclude that PDA6-1, which does not appear to contribute to the virulence of N. haematococa on pea, differs significantly from PDAT9, which is associated with high virulence.

Amino Acid Sequence↗

PubMed2005

Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides.

Calcium/calmodulin-dependent protein kinase II (CaMKII) catalyzes the phosphorylation of various cellular proteins and excessive activities have been implicated in the pathogenesis of various chronic diseases. We hypothesized that positively charged peptides can be produced through enzymatic hydrolysis of pea proteins; such peptides could then bind to negatively charged calmodulin (CaM) at a physiological pH level and inhibit CaMKII activity. Pea protein isolate was hydrolyzed with an alkaline protease (alcalase) and filtered through a 1000-mol wt cutoff membrane. The permeate, which contained low-molecular weight peptides, was used to isolate cationic peptides on an SP-Sepharose column by ion exchange chromatography. Separation of the permeate on the SP-Sepharose column yielded two fractions with net positive charges that were subsequently used for enzyme inhibition studies. Fraction I eluted earlier from the column and contained lower contents of lysine and arginine than Fraction II, which eluted later. Results show that both peptide fractions inhibited CaMKII activity mostly in a competitive manner, although kinetic data suggested that inhibition by Fraction II may be of the mixed type. Kinetic analysis (K(m) and K(i)) showed that affinity of peptides in Fraction II for CaM was more than that in Fraction I, which was directly correlated with the higher inhibitory properties of Fraction II against CaMKII. The results suggest that it may be possible to use pea protein-derived cationic peptides to modulate CaMKII activities.

Amino Acids↗

PubMed2005

Nutritional assessment of raw and germinated pea (Pisum sativum L.) protein and carbohydrate by in vitro and in vivo techniques.

OBJECTIVE: We assessed the effect of germinating Pisum sativum L. variant Arvense cv. Esla for 3 and 6 d in darkness on the chemical composition and nutritive utilization of protein and carbohydrates. METHODS: Nutritional assessment of protein and carbohydrates was based on chemical analysis of raw and germinated pea flours and in vitro and in vivo rat balance methodologies. RESULTS: Germination caused a notable decrease in alpha-galactoside content and significant increases in sucrose, glucose, and fructose. The ratio of available starch to total starch increased as a consequence of processing. The content of vitamin B2 increased significantly, whereas no significant change was observed in vitamin B1 content in germinated peas. Protein digestibility assessed with an in vivo technique (apparent digestibility coefficient) or as the percentage of dialyzable nitrogen increased significantly as a result of germination in contrast to what was observed with the in vitro pH-drop methodology. Daily food intake, nitrogen absorption and balance, percentage of retained versus absorbed nitrogen, protein efficiency ratio, and the index of available carbohydrates were significantly improved by germination for 3 d and significantly decreased by germination for 6 d. CONCLUSIONS: Germination of pea seeds for 3 d significantly improves palatability of these seeds and the nutritive utilization of protein and carbohydrates.

Animal Nutritional Physiological Phenomena↗

PubMed2005

Treatment of pea pods with Bruchin B results in up-regulation of a gene similar to MtN19.

Differential display was used to examine changes in gene expression that resulted from treatment of pea (Pisum sativum L.) with Bruchin B. This lipid-derived regulator, one of several closely related compounds collectively referred to as bruchins, is an insect elicitor that causes localized cell division and callus formation when applied to pods of pea and certain other legumes. A DNA fragment that was prominently displayed after bruchin treatment was cloned and sequenced, and a full-length cDNA was obtained. This cDNA exhibited a high degree of sequence similarity to a gene, MtN19, expressed in root nodules of Medicago truncatula Gaertn. MtN19 codes for a putative protein of unknown function that is similar in sequence to predicted proteins from a number of other plant species, both leguminous and non-leguminous. Quantitative real-time PCR showed that the expression of this MtN19-like gene was significantly up-regulated within 1.5 h of bruchin treatment, and increased more than 100-fold within 6 h of treatment. Given the rapid and strong up-regulation after exposure of pods to a bruchin, it is likely that this gene plays an important role in the response of pea to these insect elicitors.

Amino Acid Sequence↗

PubMed2005

Rapid cardiac ultrasound of inpatients suffering PEA arrest performed by nonexpert sonographers.

UNLABELLED: Cardiac arrest presenting as pulseless electrical activity (PEA) currently has a very low survival rate. Many of the conditions underlying PEA (cardiac tamponade, hypovolemia, and pulmonary embolus) are associated with specific cardiac ultrasound findings. The aim of this study was to evaluate a rapid cardiac ultrasound assessment performed by trained nonexpert sonographers integrated into the ACLS response system at a major medical center. METHODS: An emergency sonography system was created and deployed to each inpatient cardiac arrest occurring at Dartmouth Hitchcock Medical Center between November 1, 2003 and April 30, 2004. Thirteen internal medicine house officers received training to perform a limited subcostal cardiac ultrasound examination designed to diagnose cardiac tamponade, pulmonary embolus, severe hypovolemia, and lack of cardiac motion. Time from arrest alert to sonographic result, and correlation with over-reading by blinded echocardiography physicians were assessed. RESULTS: A complete emergency ultrasound examination was performed in five PEA arrests. The average time from arrest alert to interpretation was 7.75 min. (95% CI 2.8-18.3 min). Three of these examinations (60%, 95% CI 14.7-94.7%) were adequate for interpretation. Agreement between the nonexpert sonographer and echocardiography physician occurred in four of five (kappa=0.706) cases. CONCLUSION: Rapid cardiac sonography can be successfully integrated in the ACLS response. Nonexpert sonographers may be able to provide useful interpretive information when sufficiently trained.

Adult↗

PubMed2000

Characterization of the structure and expression of a highly conserved ribosomal protein gene, L9, from pea.

The eukaryotic ribosomal protein (RP) L9 is highly conserved in nature, and its gene is expressed to high levels in the actively growing tissues of pea. The transcriptional activity of the gene is highest in root, cambial and shoot meristems and immature tissues of the plant. Promoter deletion analysis using constructs employing the reporter gene gus were stably transferred into tobacco and revealed that the fully functional promoter is found in the first 316bp upstream from the start codon. Transgenic pea plants carrying one of these constructs show that translational efficiency mirrors gene transcription; gene expression appears to be developmentally regulated at the level of transcription. The coding region of the gene shares 80% amino acid homology with Arabidopsis and 76% homology with rice. Comparisons of the gene structure to that of the human, fruit fly, yeast, and Arabidopsis homologues reveal a close relationship in both promoter structure and intron insertion sites with the Arabidopsis gene. A nucleotide sequence alignment of the pea gene with other plant RP genes revealed that a sequence, -TTAGGGTTTT-, was commonly found in the forward and/or the inverted orientation at or near the TATA boxes of the promoters of these genes and may have a role in regulating the coordinate production of the RP genes in plants.

Amino Acid Sequence↗

PubMed1997

UNIFOLIATA regulates leaf and flower morphogenesis in pea.

BACKGROUND: The vegetative phenotype of the pea mutant unifoliata (uni) is a simplification of the wild-type compound leaf to a single leaflet. Mutant uni plants are also self-sterile and the flowers resemble known floral meristem and organ identity mutants. In Antirrhinum and Arabidopsis, mutations in the floral meristem identity gene FLORICAULA/LEAFY (FLO/LFY) affect flower development alone, whereas the tobacco FLO/LFY homologue, NFL, is expressed in vegetative tissues, suggesting that NFL specifies determinacy in the progenitor cells for both flowers and leaves. In this paper, we characterised the pea homologue of FLO/LFY. RESULTS: The pea cDNA homologue of FLO/LFY, PEAFLO, mapped to the uni locus in recombinant-inbred mapping populations and markers based on PEAFLO cosegregated with uni in segregating sibling populations. The characterisation of two spontaneous uni mutant alleles, one containing a deletion and the other a point mutation in the PEAFLO coding sequences, predicted that PEAFLO corresponds to UNI and that the mutant vegetative phenotype was conferred by the defective PEAFLO gene. CONCLUSIONS: The uni mutant demonstrates that there are shared regulatory processes in the morphogenesis of leaves and flowers and that floral meristem identity genes have an extended role in plant development. Pleiotropic regulatory genes such as UNI support the hypothesis that leaves and flowers derive from a common ancestral sporophyll-like structure. The regulation of indeterminancy during leaf and flower morphogenesis by UNI may reflect a primitive function for the gene in the pre-angiosperm era.

Alleles↗

PubMed1996

Macromolecular recognition: effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers.

The synthesis and binding properties of a new family of high affinity alpha-D-mannopyranoside ligands are described. The synthesis of the new multivalent ligands is based on the scaffolding of multiantennary branches of L-lysine residues having electrophilic N-chloroacetylated end groups as core structures. An alpha-D-mannopyranoside with p-substituted aryl aglycon ending with a thiol group was prepared and covalently attached to each of the branches of the dendritic structures. The resulting glycodendrimers with 2 (12), 4 (14), 8 (16), and 16 (18) mannoside residues were tested for their relative inhibitory potency by solid-phase enzyme-linked lectin assays (ELLA) using methyl and p-nitrophenyl alpha-D-mannopyranosides as standards. Concentrations necessary for 50% inhibition (IC50s) of binding of yeast mannan to Jack bean phytohemagglutinin (Canavalia ensiformis, concanavalin A) and to pea lectin (Pisum sativum) were determined. Analogous mannosylated copolyacrylamides were also prepared for comparison. The IC50 values were also plotted as a function of dendrimer valencies. The inhibitions showed 16-mer 18 to be approximately 600- and 2000-fold more potent than methyl alpha-D-mannopyranoside, and 66- and 1383-fold more potent than p-nitrophenyl alpha-D-mannopyranosides with Con A and pea lectins, respectively. Even when these numbers are expressed relative to single mannopyranoside residues per dendrimers, the relative potencies against the aromatic mannoside are still 4- and 86-fold better against Con A and pea lectins. These results unequivocally indicate that the optimum inhibitory binding properties of the new mannosylated dendrimers vary with both dendrimers and lectin valencies.

Carbohydrate Conformation↗

PubMed1998

Immunological and biochemical evidence for nuclear localization of annexin in peas.

Immunofluorescent localization of annexins using an anti-pea annexin polyclonal antibody (anti-p35) in pea (Pisum sativum) leaf and stem epidermal peels showed staining of the nuclei and the cell periphery. Nuclear staining was also seen in cell teases prepared from pea plumules. The amount of nuclear stain was reduced both by fixation time and by dehydration and organic solvent treatment. Observation with confocal microscopy demonstrated that the anti-p35 stain was diffusely distributed throughout the nuclear structure. Immunoblots of purified nuclei, nuclear envelope matrix, nucleolar, and chromatin fractions showed a cross-reactive protein band of 35 kDa. These data are the first to show annexins localized in plant cell nuclei where they may play a role in nuclear function.

Annexins↗

PubMed1994

Phototransformation of pea phytochrome A induces an increase in alpha-helical folding of the apoprotein: comparison with a monocot phytochrome A and CD analysis by different methods.

The photoreversible conformational change associated with the Pr-->Pfr transformation of a dicot phytochrome A (Pisum sativum, pea) has been probed by circular dichroism (CD) studies. Three different CD analysis methods have been used to determine the secondary structure of pea phytochrome A in both Pr and Pfr forms. We have shown that the secondary structure of dicot pea phytochrome A is very similar to the structure of monocot oat phytochrome A which was determined earlier [Sommer & Song (1990) Biochemistry 29, 1943-1948]. As with oat phytochrome A, an increase in the alpha-helical folding of the apoprotein takes place when photochrome in the Pr form is phototransformed to the Pfr form. This conformational change might well be a general characteristic of all phytochrome A's.

Apoproteins↗

PubMed2001

Production process for high-quality pea-protein isolate with low content of oligosaccharides and phytate.

A process for pea-protein isolate production, resulting in low content of phytate and oligosaccharides, has been developed. Oligosaccharides were removed from the protein fraction through ultrafiltration. Ultrafiltration of 50- and 100-kD molecular-weight cutoffs (MWCOs) were tested, and both effectively separated the oligosaccharides from the protein. Phytate degradation was achieved by incubation of the pea-protein solution by addition of exogenous phytase enzyme. An almost complete degradation of inositol hexa-, penta-, tetra-, and triphosphates was reached using an incubation time of 1 h. The reduced content of oligosaccharides and inositol phosphates is likely to result in reduced flatulence and improved mineral bioavailability. These qualities of the pea-protein isolate make it a suitable protein source for infant formula production.

Biological Availability↗

PubMed2000

Comparative investigation of concentrations of major and trace elements in organic and conventional Danish agricultural crops. 1. Onions (Allium cepa Hysam) and peas (Pisum sativum ping pong).

210 samples of onions (Allium cepa Hysam) from 11 conventionally and 10 organically cultivated sites and 190 samples of peas (Pisum sativum Ping Pong) from 10 conventionally and 9 organically cultivated sites in Denmark were collected and analyzed for 63 and 55 major and trace elements, respectively, by high-resolution inductively coupled plasma mass spectrometry. Sampling, sample preparation, and analysis of the samples were performed under carefully controlled contamination-free conditions. Comparative statistical tests of the element concentration mean values for each site show significantly (p < 0.05) different levels of Ca, Mg, B, Bi, Dy, Eu, Gd, Lu, Rb, Sb, Se, Sr, Ti, U, and Y between the organically and conventionally grown onions and significantly (p < 0.05) different levels of P, Gd, and Ti between the organically and conventionally grown peas. Principal component analysis (PCA) applied to the 63 elements measured in the individual onion samples from the 21 sites split up the sites into two groups according to the cultivation method when the scores of the first and third principal components were plotted against each other. Correspondingly, for peas, a PCA applied to the 55 elements measured as mean values for each site split up the 19 sites into two groups according to the cultivation method when the scores of the third and fourth principal component were plotted against each other. The methodology may be used as authenticity control for organic cultivation after further method development.

Food, Organic↗

PubMed2001

HPLC determination of chlorophyll and carotenoid pigments in processed green pea cultivars (Pisum sativum L.).

Chlorophyll and carotenoid pigments from six cultivars of processed green peas (Avola, Tristar, Rampart, Turon, Bella, and Greenshaft) were extracted with 100% acetone and analyzed by reversed-phase HPLC. A total of 17 pigments were identified in the pea cultivars including 8 xanthophylls ((all-E)-neoxanthin, (9'Z)-neoxanthin, (all-E)-violaxanthin, neochrome, (all-E)-lutein epoxide, (all-E)-lutein, neolutein B, neolutein A), 4 chlorophyll b related compounds (chlorophyll b derivative, chlorophyll b, chlorophyll b', and pheophytin b), 4 chlorophyll a related compounds (chlorophyll a derivative, chlorophyll a, chlorophyll a', and pheophytin a), and (all-E)-beta-carotene. The efficiency of different extraction procedures using 100% acetone showed that initial extraction followed by three reextractions without holding time between gave a higher extraction yield than no reextraction and 30 or 60 min holding time. All six cultivars contained the same pigments, but the concentration of each pigment varied significantly. On average of the two years, the chlorophyll a concentration varied from 4800 to 7300 microg/100 g fresh weight, the chlorophyll b concentration from 2100 to 2800 microg/100 g fresh weight, the (all-E)-lutein concentration from 1200 to 1900 microg/100 g fresh weight, and the (all-E)-beta-carotene concentration from 300 to 490 microg/100 g fresh weight in the processed pea cultivars. These differences in pigment concentration between the investigated cultivars are discussed in relation to maturity, product color and nutritional quality.

Carotenoids↗

PubMed2003

Nutritional evaluation of pea (Pisum sativum L.) protein diets after mild hydrothermal treatment and with and without added phytase.

The effect of mild hydrothermal treatment and the addition of phytase under optimal conditions (pH 5.5, 37 degrees C) on the nutritive utilization of the protein of pea (Pisum sativum L.) flour was studied in growing rats by examining the chemical and biological balance. Mild hydrothermal treatment produced reductions of 83, 78, and 72%, respectively, in the levels of alpha-galactosides, phytic acid, and trypsin inhibitors and also produced a significant increase in the digestive utilization of protein. The additional fall in the levels of phytic acid caused by the addition of phytase did not lead to a subsequent improvement in the digestive utilization of protein. The mild hydrothermal treatment of pea flour produced a significant increase in the metabolic utilization of protein and carbohydrates, which was reflected in the protein efficiency ratio and food transformation growth indices. These effects were not observed in the phytase-supplemented pea diet.

6-Phytase↗