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At least 775 records · Page 43Linked to original sources
PubMed1978

Polyadenylation of pea seed RNA at the early stages of germination.

1. The RNA polyadenylating activity was found in embryo axes of dry, as well as imbibed and germinated pea seeds, both in nucleus and cytoplasm. 2. The total enzymatic activity remains unchanged during germination, but the intracellular distribution is altered; the activity in nuclei is increased about four-fold at the expense of the postmitochondrial fraction. 3. Specificity towards RNA primers of the polyadenylating system from pea embryo axes is low. 4. Cordycepin inhibits RNA polyadenylation only when [14C]ATP is used as a nucleotide donor, and has no visible influence on the activity of the system utilizing [14C]oligo(A)-nucleotides. 5. It seems that RNA in the pea embryo axes is polyadenylated by a two-step mechanism: synthesis of oligo(A)-nucleotides, and their addition to RNA.

Deoxyadenosines↗
PubMed1986

Production of pea lectin in Escherichia coli.

In order to explore the molecular basis for the glycopeptide specificity of legume lectins, we have developed an experimental system in which specific amino acid alterations can be introduced into the carbohydrate binding site of pea lectin. This system is based on the production of pea lectin in Escherichia coli. The plasmid coding for the lectin was constructed from two lectin cDNA sequences isolated from Pisum sativum seeds (Higgins, T. J. V., Chandler, P. M., Zurawski, G., Button, S. C., and Spencer, D. (1983) J. Biol. Chem. 258, 9544-9549) and an expression vector based on the gene for the outer membrane lipoprotein of E. coli (Nakamura, K., and Inouye, M. (1982) EMBO J. 1, 771-775). The lectin is produced as a single polypeptide chain and forms insoluble aggregates in E. coli cells (2-5 mg/liter). Functional lectin is recovered by solubilization of the aggregates in guanidinium hydrochloride, renaturation in the presence of MnCl2 and CaCl2, and affinity purification on Sephadex. This procedure yields a homogeneous 28,000-dalton protein. Comparison of the recombinant lectin with natural pea lectin in an inhibition of hemagglutination assay demonstrated that there is no detectable difference in the carbohydrate binding properties of the two lectins.

Amino Acid Sequence↗
PubMed1986

Gene structure, protein structure, and regulation of the synthesis of a sulfur-rich protein in pea seeds.

Two low molecular weight pea seed albumins (Mr approximately 6000 and approximately 4000) have been characterized by protein, cDNA, and gene sequencing. Both proteins are encoded by separate regions of the same mRNA species. The initial translation product is a preproprotein from which a signal sequence is removed co-translationally. The resultant proprotein (PA1) is then cleaved post-translationally to yield the mature form of the two albumins (PA1a and PA1b). Comparison of cDNA and protein sequences suggests that at least four different PA1 genes are expressed in the pea genome. Both PA1a and PA1b have an unusually high cysteine content (7.5 and 16.2%, respectively). Pea seeds developing under suboptimal levels of sulfur nutrient supply contain reduced levels of PA1 mRNA and accumulate greatly reduced levels of PA1a and PA1b in the mature seed. In vitro transcription studies showed that this reduced level of PA1 mRNA resulted from reduced post-transcriptional stability rather than an altered rate of transcription of the PA1 gene. In contrast, during normal seed development, the level of PA1 mRNA seems to be under transcriptional control. Sequence comparisons reveal some homology between PA1 and a number of low molecular weight proteins from seeds of a wide range of mono- and dicotyledonous plants.

Albumins↗
PubMed1979

On alcohol dehydrogenase activity in aged pea seeds.

Inhibitory substances (or substance) of alcohol: NAD oxidoreductase activity are present in petroleumbenzin extracts of both less than 1-year-old and 8-year-old pea seeds. The inhibitory effect is very strong when petroleumbenzin extracts of "old" pea seeds are used, only mild in the case of "young" pea seeds. These results suggest a relatioship between the inhibitory substances and ageing of the seeds.

Age Factors↗
PubMed1984

Evidence for the selective replication of dwarf pea DNA evoked by exogenous gibberellin application.

Characteristics of the total DNA preparations isolated from apical parts of dwarf pea seedlings untreated and treated with gibberellic acid (GA3) were compared. Analytical centrifugation in a self-generated CsCl density gradient revealed the occurrence of a heavy satellite DNA band (p = 1.712 g X cm-3) in addition to the main DNA band (p = 1.696 g X cm-3) in the DNA preparation extracted from GA3-treated seedlings, that could not be detected in the DNA isolated from untreated plants. The existence of this GC-rich DNA fraction was additionally confirmed by means of derivative DNA melting profiles. Comparison of the reassociation kinetics obtained for control DNA with DNA from GA3-treated plants showed changes in the percentage distribution of three main DNA sequence classes, with different repetition frequency in the haploid pea genome. It is postulated that such a variation in the percentage of different C0t families might reflect the selective DNA replication evoked by hormonal treatment of dwarf pea plants.

Base Sequence↗
PubMed1984

Subcellular localization of hexokinase in pea leaves. Evidence for the predominance of a mitochondrially bound form.

Hexokinase (ATP: D-hexose-6-phosphotransferase, EC 2.7.1.1) activity was determined in subcellular fractions prepared from pea (Pisum sativum) leaf homogenates. About 60% of the total detectable activity of hexokinase was found associated with a particulate fraction consisting essentially of mitochondria and chloroplasts and free of cytosol contamination. The hexokinase specific activity of the particulate fraction was 2-fold higher than that of the homogenate and about 4-fold higher than that of the cytosol. Using a specially designed isokinetic-isopycnic sucrose density gradient centrifugation method, the distribution of hexokinase activity correlated with that of the mitochondrial marker (cytochrome oxidase) and not with that of the chloroplast membrane marker ( chlorophyll ) or that of the cytosol marker (phosphoenolpyruvate carboxylase). Thus, the hexokinase/mitochondria ratio was close to 1.0 along the entire gradient, while the hexokinase/chloroplast ratio varied over a 10-fold range. The results strongly suggest that hexokinase is predominantly bound to mitochondria of pea leaves, and that pea leaf chloroplasts are essentially devoid of any specifically associated hexokinase activity. This work provides the first demonstration of a specific association of hexokinase with mitochondria from photosynthetic tissues of higher plants.

Centrifugation, Isopycnic↗
PubMed1983

Intracellular sites of synthesis and processing of lectin in developing pea cotyledons.

The biosynthesis and processing of pea lectin was studied in developing pea cotyledons by a combination of pulse-chase experiments using 14C-aminoacids and subcellular fractionation of the homogenates. Lectin polypeptides were isolated on immunoaffinity gels and fractionated on sodium dodecyl sulfate-polyacrylamide gels followed by fluorography. Whether made in vivo or in an in vitro chain completion system containing polysomes still attached to microsomal membranes, newly synthesized lectin had an Mr of 23,000. In vivo labeling showed that radioactive lectin first associates with the rough endoplasmic reticulum and is then sequestered into the lumen of the endoplasmic reticulum. Pulse-chase experiments showed that it is chased out of the endoplasmic reticulum considerably more slowly than the storage proteins and accumulates in the protein bodies, initially as a polypeptide of Mr = 23,000. This pro-lectin is processed in the protein bodies to its mature form with polypeptides of Mr = 17,000 and 6,000. Pea lectin is synthesized throughout the protein accumulation phase of seed formation with maximum levels of synthesis and of mRNA approximately half-way through this period.

Endoplasmic Reticulum↗
PubMed1980

Mass spectral identification and gas-liquid chromatographic determination of methyl 4-chloroindolyl-3-acetate in canned and frozen peas.

Methyl 4-chloroindolyl-3-acetate (MCIA), a naturally occurring auxin, has been identified in canned and frozen peas by gas-liquid chromatography (GLC)/mass spectrometry. Eight samples were analyzed for MCIA using slightly modified official AOAC multiple pesticide residue procedures employing GLC with microcoulometric detection. Levels of MCIA averaged 0.20 ppm for canned peas and 0.16 ppm for frozen peas. Recovery of MCIA from a fortified sample was 40%.

Chromatography, Gas↗
PubMed1995

[Central mechanism of inhibitory effect of histamine H1-receptor agonists PEA on gastric acid secretion].

The present experiment is undertaken to study the central mechanism of the inhibitory effect of 2-pyridylethylamine (PEA, i.c.v.) on the gastric acid secretion. Gastric acid was continuously washed out with 37 degrees C saline by means of a perfusion pump in male adrenalectomized wistar rats. Drugs were injected into the third ventricle to examine the effect on pentagastrin-induced (160 micrograms/kg, s.c.) gastric acid secretion. The results were as follows: (1) Pretreatment with CRF-antiserum (2.5 microliters, 1:20,000, i.c.v.) blocked the inhibitory effect of PEA (10 micrograms, i.c.v.) on gastric acid secretion. (2) Administration of CRF (1 and 2 micrograms, i.c.v.) or beta-endorphin (0.94 and 1.25 micrograms, i.c.v.) markedly inhibited the gastric acid secretion. (3) Pretreatment with naloxone (5 micrograms, i.c.v.) blocked the inhibitory effect of CRF (1 microgram, i.c.v.), but the inhibitory effect of beta-endorphin (0.94 microgram, i.c.v.) was not changed by pretreatment with CRF-antiserum (1:20,000, 2.5 microliters, i.c.v.). These results suggest that PEA stimulates the release of hypothalamic CRF which stimulates the release of hypothalamic endogenous opioid peptides. The peptides again induces vagus nerve-mediated inhibitory effect on gastric acid sceretion.

Adrenalectomy↗
PubMed1994

Resistance of green peas to legume viruses.

A total of 16 green pea cultivars (Pisum sativum L.) were screened for resistance to bean yellow mosaic virus (BYMV), pea enation mosaic virus (PEMV), and alfalfa mosaic virus (AMV). Cvs. Avola, Midget, Wawerplus, Wawerex, Bunny and Banff were found immune to BYMV infection. Cvs. Marx and Pion exhibited a high level (above 95%) of resistance to BYMV, but they were highly susceptible to PEMV and AMV. It is recommended to use BYMV-immune or highly BYMV-resistant cultivars for further breeding. There were no significant differences in AMV levels among the respective pea cultivars.

Alfalfa mosaic virus↗
PubMed1994

Purification and characterization of a eukaryotic type 1 topoisomerase from pea chloroplast.

A 69-kDa protein with topoisomerase I activity has been homogeneously purified from the chloroplasts of pea leaves. The topoisomerase properties are detected in crude lysate of pea chloroplasts using the technique of transferring 32P radioactivity from the 32P-labeled DNA to the protein. The purified enzyme relaxes both positive and negative supercoils in topological steps of unity without requiring magnesium ions. The enzyme is sensitive to topoisomerase I-specific inhibitors like camptothecin and berenil, and unaffected by reagents like novobiocin and doxorubicin at the topoisomerase II-inhibitory dosage. In the presence of the enzyme, supercoiled DNA is nicked, and the 3'-phosphoryl end of the nick becomes covalently linked with the enzyme. A tyrosine residue of the enzyme is responsible for the covalent linkage. Rabbit antiserum raised against the 16-mer peptide spanning the active residues of human topoisomerase I recognizes the 69-kDa protein within the crude lysate of pea chloroplasts as does the antiserum to the purified 69-kDa protein. From the enzymatic characteristics, the protein has been classified as a eukaryotic type I topoisomerase.

Amino Acid Sequence↗
PubMed1993

Effects of pea and soybean fibre on postprandial lipaemia and lipoproteins in healthy adults.

To evaluate some possible mechanisms whereby total dietary fibre (TDF) may affect lipid metabolism in humans, six normolipidaemic males ingested on separate days a low-fibre test meal (2.8 g TDF) containing 70 g fat and 756 mg cholesterol, enriched with 10 g TDF in the form of either pea fibre or soybean fibre. Fasting and post-meal blood samples were obtained for 7 h and chylomicrons (CM) were isolated. Lipoproteins (VLDL+CM remnants, LDL, HDL) were isolated from the baseline samples and the samples of the 2-3 h triglyceride peaks. As compared to the postprandial response given by the control low-fibre test meal, adding fibre induced no change in serum glucose, insulin or Apo A1 and Apo B variations. The serum triglyceride response was not altered by adding fibres but the 2-3 h chylomicron triglyceride rise was increased (P < or = 0.05) by soybean fibre. VLDL+CM remnants, LDL and HDL triglyceride variations were unchanged with fibres. Cholesterolaemia decreased postprandially for 6 h, and was further lowered in the presence of pea fibre. This resulted from a marked decrease in serum esterified cholesterol. The chylomicron cholesterol and phospholipid rise was lowered in the presence of either fibre. The postprandial changes in the free cholesterol concentrations of the various lipoprotein classes were not altered by fibre whereas changes from baseline in esterified cholesterol concentrations were reduced by soybean fibre in LDL and amplified by soybean and pea fibres in HDL. The results obtained show that dietary fibre present in legumes may alter postprandial lipaemia and lipoproteins in humans to a variable extent. These effects could be related to some long-term metabolic effects.

Adult↗
PubMed1996

Crop improvement and disease suppression by a Bacillus spp. SR2 from pea nut rhizosphere.

An antibiotic producing Bacillus strain SR2, isolated from pea nut rhizosphere, showed in vitro antibiosis against many known plant pathogens. Seed bacterization with this strain showed an enhancement in seed germination, shoot height, root length, fresh and dry weights in four crop plants. A multiple drug resistant strain, SR2+, used to monitor root colonization confirmed the root colonization by the organism. Seed bacterization, reduced the number of chick pea wilted plants in wilt-sick soil, making the organism a potential bio-control agent against chick pea wilt.

Anti-Bacterial Agents↗
PubMed1977

Pea histones H2A and H2B. Variable and conserved regions in the sequences.

Pea histone II group, a mixture of H2A and H2B obtained by chromatography on an ion-exchange resin, was further fractionated by carboxymethylcellulose chromatography and purified by Bio-Gel P-60 chromatography. Their chromatographic behaviors and gel electrophoretic mobilities of single bands differed significantly from those of calf H2A and H2B. Their amino acid compositions were similar to those of the calf histones as a whole, but differed in detail in certain respects. The partial sequence of pea H2B was deduced from the amino acid compositions of BrCN cleavage fragments and tryptic peptides in comparison with the known sequence of calf H2B. It is different in the amino-terminal basic region from the calf H2B, with a blocked amino terminal and a larger number of residues. In contrast, the middle and carboxy-terminal hydrophobic regions are relatively similar, with at least 19-21 different residues and microheterogeneity at two positions of the pea sequence. The sequence of H2A may vary in much the same way as that of H2B, as suggested by the similar extent of differences in their amino acid compositions. It is thus assumed that the amino-terminal regions, at least, of H2A and H2B histones are variable in evolution provided that they remain basic enough to bind DNA, whereas the middle and carboxy-terminal hydrophobic regions of H2A, H2B, H3, and H4 should be conserved to ensure precise histone core formation inside the repeated units of chromatin.

Amino Acid Sequence↗
PubMed1997

Effect of calcium on RNA content in meristematic cells of pea (Pisum sativum L.) roots treated with toxic metals.

RNA content in nucleolus, nucleus and cytoplasm in meristematic cells of pea roots growing for 144 h in the presence of calcium and/or toxic metals (Cd2+, Cr3+, Pb2+) was examined using cytophotometric procedures, after staining with gallocyanine. The effect of treatment with tested metals was twofold: on the one hand, it considerably reduced RNA content in the nucleolus, on the other it enhanced RNA level in the nucleus and most visibly in the cytoplasm, resulting in the increase in total amount of RNA in cells of pea roots. The presence of calcium in metal solutions in different ways affected RNA content in meristematic cells of pea. In roots treated with cadmium, the addition of calcium ions diminished the toxic effect of that metal, as demonstrated by an increase in RNA content in the nucleolus, although reduction of RNA amount in the nucleus, cytoplasm and in whole cell was observed. A clearly stimulative effect of calcium was noted in material grown in the presence of chromium or lead, where a high increase in RNA content in nucleolus, nucleus and cytoplasm took place.

Cadmium↗
PubMed1976

Further characterization of a low-molecular weight allergen fragment isolated from the green pea.

A low molecular weight allergen fragment present in the pea dialysate fraction was purified by ion-exchange chromatography and gel filtration. The highly purified allergen fragment inhibits both antigen-indiced passive cutaneous anaphlaxix reactions in guinea-pigs sensitized with rabbit anti-pea extract sera and Prausnitz-Küstner reactions in non-allergic volunteers sensitized with the sera of patients sensitive to green peas. Preliminary analysis of the purified allergen fragment indicates that it is a glycoprotein with a molecular weight of 1800 +/- 250.

Allergens↗
PubMed2025

Analysis of duplication and possible sub-functionalization of wing gene network components in pea aphids.

A fundamental focus of evolutionary-developmental biology is uncovering the genetic mechanisms responsible for the gain and loss of characters. One approach to this question is to investigate changes in the coordinated expression of a group of genes important for the development of a character of interest (a gene regulatory network). Here we consider the possibility that modifications to the wing gene regulatory network (wGRN), as defined by work primarily done in Drosophila melanogaster, were involved in the evolution of wing dimorphisms of the pea aphid (Acyrthosiphon pisum). We hypothesize that this may have occurred via changes in expression levels or duplication followed by sub-functionalization of wGRN components. To test this, we annotated members of the wGRN in the pea aphid genome and assessed their expression levels in first and third nymphal instars of winged and wingless morphs of males and asexual females. We find that only two of the 32 assessed genes exhibit morph-biased expression. We also find that three wing genes (apterous (ap), warts (wts), and decapentaplegic (dpp)) have undergone gene duplication. In each case, the resulting paralogs show signs of functional divergence, exhibiting either sex-, morph-, or stage-specific expression. Two gene duplicates, wts2 and dpp3, are of particular interest with respect to wing dimorphism, as they exhibit a wingless male-specific isoform and wingless male-biased expression, respectively. These results supplement our understanding of trends in developmental gene network evolution, such as side-stepping pleiotropic constraint via duplication and sub-functionalization, underlying the emergence of novel phenotypes.

dimorphism↗
PubMed2001

Isolation and study of the functional properties of pea proteins.

Proteins of pea seeds were isolated after defatting with hexane using alkaline (0.1 M sodium hydroxide) extraction and acid (HCl) precipitation. Concentrates were also prepared by hexane extraction and ethanolic extraction (pH = 5). Gross chemical composition amino acid content and functional properties (solubility profile, emulsifying--and foaming properties, water--and oil absorption) were studied. The results were compared with the same parameters of soy and lupin protein products. Although the majority of functional characteristics of isolates were lower in comparison to soy isolates, pea protein concentrate and isolate could be successfully used in bakery products for enrichment in protein and improvement of biological value. Their utilization as meat protein substitute in some Frankfurter type sausages is also possibly.

Amino Acids↗