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PubMed1977

The carbon monoxide-binding hemoprotein reducible by hydrogen peroxide in microsomal fractions of pea seeds.

There exist at least two kinds of CO-binding hemoproteins in microsomal fractions of germinating pea (Pisum sativum) seeds. One of them is cytochrome P-450 and the other is also a protoheme protein (judged from its pyridine hemochrome spectrum), which is not hitherto reported. The content of the new hemoprotein is much higher than that of cytochrome P-450 in the early stage of germination. During germination the former decreases and the latter increases. The new hemoprotein is not appreciably reduced by sodium dithionite alone within a few minutes, but, it is easily reduced by dithionite in the presence of methyl viologen and also by hydrogen peroxide when CO is present. The addition of hydrogen peroxide to pea microsomes in the absence of CO causes destruction of the hemoprotein and also decolorization of endogenous carotenoid. Destruction of these components is brought about by organic hydroperoxides independently of the presence of CO. In the presence of hydroxylamine, the addition of hydroperoxides to the microsomes results in the formation of an absorption spectrum similar to the spectra of ferrous-NO complexes of protoheme proteins. When N,N-dimethyl p-phenylenediamine is present, the reaction of pea microsomes with hydroperoxides gives a spectrum similar to that of the ferryl form of myoglobin. The reactions of the hemoprotein with hydroperoxides are inhibited by alpha,alpha'-dipyridyl and aniline, with which pea microsomes form binding spectra. The microsomes form a rather stable difference spectrum with hydroxylamine. However, the hemoprotein is destroyed when hydroxylamine is added to the microsomes in the reduced state.

Carbon Monoxide↗

PubMedDate not supplied

Liquid chromatographic determination of alpha-solasonine in frozen green peas as an indicator of the presence of nightshade berries.

Nightshade berries containing glycoalkaloids can be a contaminant in green peas. Methodology was developed to detect this contamination. The glycoalkaloid alpha-solasonine was extracted from frozen green peas with 1% (v/v) acetic acid, cleaned up on a C18 cartridge, and determined by liquid chromatography with UV detection at 200 nm. Method performance characteristics for the determination of alpha-solasonine include linearity from 140 to 1500 ng injected (r = 0.9996-0.9999); recovery ranging from 68 to 79%; limit of quantitation (LOQ) = 4.5 ppm (280 ng standard), and limit of detection = 0.64 ppm (40 ng standard). At the LOQ, the expanded uncertainty at 95% confidence was 0.38 x the reported value. The method was applied to the detection of alpha-solasonine in frozen green peas in a 2-year study of 60 samples of frozen green peas from Ontario, Canada. None of the samples contained alpha-solasonine. No unripe berries of Solanum nigrum were detected visually in the samples.

Chromatography, Liquid↗

PubMed2003

Expression of PIN and AUX1 genes encoding putative carrier proteins for auxin polar transport in etiolated pea epicotyls [correction of epicotyles] under simulated microgravity conditions on a three-dimensional clinostat.

Etiolated pea (Pisum sativum L. cv. Alaska) seedlings grown under simulated microgravity conditions on a 3-dimensional clinostat showed automorphosis-like growth and development similar to that observed in true microgravity conditions in space. Application of inhibitors of auxin polar transport phenocopied automorphosis-like growth on 1 g conditions, suggesting that automorophosis is closely related to auxin polar transport. Strenuous efforts to know the relationships between automorphosis and auxin polar transport in pea seedlings at molecular bases resulted in successful identification of PsPIN2 and PsAUX1 encoding putative auxin efflux and influx carrier protein, respectively. Significantly high levels in homology were found on nucleotide and deduced amino acid sequences among PsPIN2, PsPIN1 and AtPINs, and between PsAUX1 and AtAUX1. Expression of PsPIN1 and PsAUX1 genes in etiolated pea seedlings grown on the clinostat were substantially affected, but that of PsPIN2 was not. Roles of these genes in auxin polar transport and automorphosis of etiolated pea seedlings are also described.

Biological Transport↗

PubMed2005

A CAPS marker set for mapping in linkage group III of pea (Pisum sativum L.).

A set of twelve CAPS markers was mapped for linkage group III of pea (Pisum sativum L.). New primers were designed to use a polymerase chain reaction to amplify fragments of sequenced pea genes containing at least one large intron. Amplification products were tested for polymorphism across three pea lines (Chi115, Flagman and WL1238) using eleven four-base restriction endonucleases. Nine STS markers for linkage group III from the literature were also tested for polymorphism, and five of these were used in this mapping study as anchor points. All polymorphic loci were located by genetic analysis of the F(2)population from the cross Chi115 x WL1238, and a map of linkage group III consisting of one morphological and twelve CAPS markers was created. The map covers the full length of the chromosome and is about 162 cM long. All the CAPS markers in a set were used to test for polymorphism among 10 additional pea DNA samples extracted from different marker lines and cultivars.

Chromosome Mapping↗

PubMed2005

[Identification and mapping of polymorphic RAPD markers of pea (Pisum sativum L.) genome].

Various pea cultivars, lines, and mutants were studied by the RAPD method. Polymorphic fragments characteristic of certain pea genotypes and which can be used for identifying genotypes were detected. Inheritance of some polymorphic RAPD fragments was studied. Mendelian inheritance of these fragments was shown. By analyzing the data obtained in studies of RAPD polymorphism, genetic distances between different pea cultivars, lines, and mutants were calculated and a genealogic dendogram showing a varying extent of differences between RAPD patterns was constructed. Ten new RAPD markers linked to various pea genes were detected. Genetic distances between RAPD markers and genes to which they are linked were calculated, and the respective disposition of RAPD markers on chromosomes was established.

Chromosome Mapping↗

PubMed2005

Efficiency of transformation of Polish cultivars of pea (Pisum sativum L.) with various regeneration capacity by using hypervirulent Agrobacterium tumefaciens strains.

An Agrobacterium-mediated transformation method of pea has been developed for several edible and fodder cultivars of pea (Pisum sativum L.), characterized previously in their potential for regeneration via organogenesis. The most appropriate explant, which was susceptible to Agrobacterium infection and capable of regenerating transgenic plants, turned out to be a slice of an immature embryo, including the embryo axis and the basal part of a cotyledon. Three hypervirulent strains of A. tumefaciens were tested: AgL0, AgL1 and EHA105. Each carried the binary vector pP35SGIB containing the uid gene, with an intron under control of the 35S promoter, and the bar gene conferring resistance to phosphinotricin. Strain AgL0 was found to be efficient for the majority of cultivars, followed by AgL1 and EHA105. Transformation efficiency varied from 0.7 to 4.1%, depending on cultivar and Agrobacterium strain. The transformation efficiency of particular pea cultivars did not clearly correspond to their regeneration capacity, which--although indispensable--was not a critical parameter of successful transformation. The presence of integrated genes in pea genomic DNA was detected by the PCR. T-DNA was stably transmitted to the progeny, as it was confirmed by Southern hybridization. The activity of introduced genes was analysed by the histochemical GUS assay and by painting leaves or by spraying transgenic plants with the herbicide Basta.

Aminobutyrates↗

PubMed1992

Identification and localization of multiple forms of serine hydroxymethyltransferase in pea (Pisum sativum) and characterization of a cDNA encoding a mitochondrial isoform.

Serine hydroxymethyltransferase (SHMT) has been purified from the mitochondria of green pea leaves. Activity can be fractionated into two distinct peaks by ion exchange chromatography. While these two forms of the enzyme are immunologically indistinguishable, immunoinhibition experiments show the presence of a distinct non-mitochondrial third form of the enzyme to also be present in green pea leaves. While this mitochondrial form of SHMT is abundant in leaves it is absent from roots, although the two tissues have comparable SHMT activity. An antibody raised to purified mitochondrial SHMT was used to screen a cDNA expression library. The sequence of one of the isolated positive clones contained an open reading frame, which encoded a sequence that matched the amino acid sequence determined from the N terminus of the mature protein. The open reading frame encodes a mature protein of 487 amino acids with a M(r) of 54,000, together with a 27-31 amino acid serine-rich leader sequence, presumably required for mitochondrial targeting. The cDNA hybridizes to a small multigene family of 2-3 genes, which appear to be expressed predominantly in leaves. Comparison of the deduced amino acid sequence with the amino acid sequences of the rabbit mitochondrial and cytoplasmic SHMT, show that pea mitochondrial SHMT is equally similar to both of these enzymes. In addition, the rabbit sequences are more like one another than they are to the pea sequence, suggesting an interesting evolutionary relationship for these proteins.

Amino Acid Sequence↗

PubMed2005

[Investigation of chromosomes in varieties and translocation lines of pea Pisum sativum L. by FISH, Ag-NOR, and differential DAPI staining].

The DNA intercalator 9-aminoachridine was used for obtaining high-resolution DAPI patterns of chromosomes of Pisum sativum L. with more than 300 bands per haploid chromosome set. The karyotypes of three pea varieties, Viola, Capital, and Rosa Crown, and two translocation lines, L-108 (T(2-4s)) and M-10 (T(2-7s)), were examined. Based on the results of DAPI staining, we have identified chromosomes, constructed idiograms, and established breakpoints of chromosome translocations. Lines L-108 (T(2-4s)) and M-10 (T(2-7s)) were shown to appear as a result of respectively one translocation between chromosomes 2 and 4 and two translocations between chromosomes 2 and 7. All varieties and translocation lines of pea were examined using fluorescence in situ hybridization (FISH) with telomere repetition probes, 5S and 45S wheat DNA probes. Transcriptional activity of 45S rRNA was detected by Ag-NOR staining. Telomere repetitions were shown to be located only in telomeric chromosome regions. Using high-resolution DAPI staining allowed us to verify localization of 5S genes on pea chromosomes 1, 3, and 5. 45S rDNAs were localized in the secondary constriction regions on the satellite and the satellite thread of chromosome and on the satellite thread and in more proximal satellite heterochromatic region of chromosome 7. The size of 45S rDNA signal on chromosome 7 was larger and its transcriptional activity, higher than the corresponding parameters on chromosome 4 in most of the forms studied. A visual comparison of the results of FISH and Ag-NOR staining of normal and translocated pea chromosomes did not reveal any significant differences between them. The translocations of the satellite chromosomes apparently did not cause significant changes either in the amount of the ribosomal genes or in their transcriptional activity.

Chromosome Banding↗

PubMed1975

Studies on phytohemagglutinins. XXIV. Isoelectric point and hybridization of the pea (Pisum sativum L.) isophytohemagglutinins.

The isoelectric point of the two pea isophytohemagglutinins varies from pH 5.7 to pH 8.4 depending on the composition of the buffer used. Isoelectric focusing reveals three main molecular species with pI at pH 5.90, 6.35 and 7.00. Molecular species with pI at pH 5.9 and 7.0 correspond to the two pea isophytohemagglutinins which can be obtained by DEAE-cellulose chromatography (Entlicher, G., Kostír, J.V. and Kocurek, J. (1970) Biochim. Biophys. Acta 221, 272-281). A molecular species with pI at pH 6.35 is formed from the two pea isophytohemagglutinins by hybridization. According to the hybridization pattern and subunit composition of the pea isophytohemagglutinins the subunit composition AABB, AACC and AABC can be proposed for the three molecular species with respect to ionic properties of the subunits.

Buffers↗

PubMed1986

The crystal structure of pea lectin at 3.0-A resolution.

The structure of pea lectin has been determined to 3.0-A resolution based on multiple isomorphous replacement phasing to 6.0-A resolution and a combination of single isomorphous replacement, anomalous scattering, and density modification to 3.0-A resolution. The pea lectin model has been optimized by restrained least squares refinement against the data between 7.0- and 3.0-A resolution. The final model at 3.0 A gives an R factor of 0.24 and a root mean square deviation from ideal bond distances of 0.02 A. The two monomers in the asymmetric unit are related by noncrystallographic 2-fold symmetry to form a dimer. Monomers were treated independently in modeling and refinement, but are found to be virtually identical at this resolution. The molecular structure of the pea lectin monomer is very similar to that of concanavalin A, the lectin from the jack bean. Similarities extend from secondary and tertiary structures to the occurrence of a cis-peptide bond and the pattern of coordination of the Ca2+ and Mn2+ ions. Differences between the two lectin structures are confined primarily to the loop regions and to the chain termini, which are different and give rise to the unusual permuted relationship between the pea lectin and concanavalin A protein sequences.

Concanavalin A↗

PubMed1979

[Effects of specific reagents and urea on the reactivity of non-heme iron and thiol groups of pea and corn ferredoxins].

The reactivities of the SH-groups of pea and corn ferredoxins were found to be different. One or two SH-groups in the molecule of pea ferredoxin and one SH-group in the molecule of corn ferredoxin are readily available for the thyol group specific reagents. Four SH-groups of both ferredoxins are completely masked, i. e. available for the thyol reagents only after protein denaturation in the presence of urea. The rates of SH-group interaction with the sulfhydryl reagents in corn ferredoxin are lower than those in pea ferredoxin. The non-haem iron of pea ferredoxin interacts with the complex formers far more rapidly as compared to corn ferredoxin. The ferredoxins tested differ in the amount of iron atoms. The latter require the presence of oxygen for their complete interaction with the complex formers.

Ferredoxins↗

PubMed1980

Intraspecies variability in transmission efficiency of stylet-borne viruses by the pea aphid (Acyrthosiphon pisum).

The efficiency of bean yellow mosaic virus (BYMV; Potyvirus group) tranasmission from pea to pea plants by 36 clones of the pea aphid (Acyrthosiphon pisum) was studied. The efficiency of the clones varied; it was not related to the aphid colour form (green, red or yellow) or the origin of the clone (host plant, geographic area). With alfalfa mosaic virus, the virus-vector relationships concerning transmission efficiency were, in general, similar to those found with BYMV. The behaviour of the clones to the circulative pea enation mosaic virus was, however, different.

Aphids↗

PubMed1984

[Kinetics of thermal inactivation of peroxidases in turnips and peas].

The heat inactivation of peroxidase in green peas and turnips grown in Venezuela was determined experimentally at temperatures ranging from 60 degrees C to 76 degrees C for turnips, and between 72 degrees C and 82 degrees C for green peas. The thermal destruction curves obtained were found to be biphasic, following first-order kinetics of inactivation, and with average times for the change of phase of 22.5 sec and 23.8 sec for the turnips and peas, respectively. The activation energies, as calculated by the Arrhenius equation for the first and second inactivation intervals, were 27.1 kcal/mole and 43.5 kcal/mole for turnips, and 34.5 kcal/mole and 28.9 kcal/mole for green peas.

Fabaceae↗

PubMed1983

The biosynthesis and primary structure of pea seed lectin.

Isolation of pea lectin from immature seeds, together with in vivo pulse-chase labeling and in vitro translation of RNA from such seeds, all gave results which indicated strongly that pea lectin is initially synthesized as a large precursor (pre-pro-form) (Mr = 25,000) which is cleaved both co- and post-translationally to yield the alpha and beta subunits of mature lectin. Two overlapping cDNA plasmids complementary to lectin mRNA were sequenced. They coded for both beta and alpha subunits of lectin, in the orientation beta leads to alpha from the NH2 terminus, together with a hydrophobic NH2-terminal leader sequence and included a 3' untranslated region of 124 nucleotides. In the appropriate reading frame, no stop codon was found between the coding sequences for the beta and alpha subunits, confirming the synthesis of pea lectin via a pre-pro-form. The entire pea lectin sequence showed a high degree of homology with the published amino acid sequences of lectins from lentil, broad bean, and, to a lesser extent, with concanavalin A from jack bean. Sequence variation occurred mainly in those regions thought not to be involved in metal- and sugar-binding or in the formation of beta-pleated sheets.

Amino Acid Sequence↗

PubMed1995

Nucleoside diphosphate kinase from pea chloroplasts: purification, cDNA cloning and import into chloroplasts.

Nucleoside diphosphate kinase (NDPK; EC 2.7.4.6) was enriched 1900-fold from purified pea (Pisum sativum L. cv. Golf.) chloroplasts. The active enzyme preparation contained two polypeptides of apparent molecular weight 18.5 kDa and 17.4 kDa. Both proteins were enzymatically active and were recognized by an antiserum raised against NDPK from spinach chloroplasts, suggesting the existence of two isoforms in pea chloroplasts. The N-terminal protein sequence data were obtained for both polypeptides and compared with the nucleotide sequence of a cDNA clone isolated from a pea cDNA library. The analysis revealed that the two NDPK forms are encoded for by one mRNA, indicating that the lower-molecular-weight form could represent a proteolytic breakdown product of the 18.5-kDa NDPK. The pea chloroplastic NDPK is made as a larger precursor protein which is imported into chloroplasts. The NDPK precursor is then processed by the stromal processing peptidase to yield the 18.5-kDa form.

Amino Acid Sequence↗

PubMed1994

Functional analysis of the promoters of phenylalanine ammonia-lyase genes in pea.

Pycnospore germination fluid of Mycosphaerella pinodes, a fungus pathogenic on pea, contains both an elicitor and a suppressor of the accumulation of pisatin, a major phytoalexin of pea. Transcription of the genes encoding key enzymes in the biosynthesis of pisatin, namely PAL (a gene encoding phenylalanine ammonia-lyase) and CHS (a gene encoding chalcone synthase), was shown to be activated upon the treatment of pea epicotyl tissues with the fungal elicitor and suppressed upon treatment with the fungal suppressor. To investigate the mechanisms underlying activation and suppression of plant defense genes by signal molecules secreted by a fungal pathogen and other stresses, such as ultraviolet (UV) light, we constructed chimeric genes composed of the 5'-flanking regions of two members of the PSPAL family (the genes encoding phenylalanine ammonia-lyase in Pisum sativum) fused to a bacterial gene for chloramphenicol acetyltransferase. Then, the cis-regulatory elements necessary for elicitor-mediated activation and suppressor-mediated suppression were examined in pea protoplasts. Functional analysis of 5' nested deletions of PSPAL1 and PSPAL2 suggested that an enhancer-like element is located in the TATA-distal region (-2,196 to -406) in PSPAL2. A cis-acting element(s) responsible for elicitor-mediated activation was found in the TATA-proximal region (-340 to -95 in PSPAL1; -406 to -158 in PSPAL2), in which the consensus sequence motifs known as box 1, box 2 and box 4 [Yamada et al. (1992) Plant Cell Physiol. 33: 715, Lois et al. (1989) EMBO J. 8: 1641] were present in close proximity. Furthermore, both promoters were activated by UV light but were partially suppressed in response to the fungal suppressor.

Ascomycota↗

PubMed1993

[Preparation of flour processed with pigeon pea seed].

Pigeon pea is a legume grain of good production capacity and of a relatively high nutritive value, which has not been used in Latin America on the basis of the potential it offers. In this study experiments were conducted to learn about the possibility of processing pigeon pea to yield an intermediate flour with good functional characteristics for food product development. The intermediate pigeon pea flour was produced through a selection of a process to efficiently dehull the grain followed by a thermic process to improve its functional properties and nutritive value. The best dehulling process was subjecting the grain to a vapor treatment for five minutes, followed by a 2-hour dehydration of surface moisture with air at 60 degrees and dehulling with an 8-disc dehuller for 10 minutes. Yield was 84% with 70.7% dehulling efficiency. Pigeon pea flours were prepared by three thermic processes: pressure cooking at 15 lb (121 degrees C) for 5 and 10 minutes as a reference product; cooking and drying with a drum dryer at 120 degrees C and 4 rpm and by extrusion-cooking with the material with 18 and 21% moisture at 270 and 300 degrees F, respectively. Process selection was based on the functional properties such as water absorption index, water solubility index, soluble nitrogen and viscosity, through chemical analysis of protein, available lysine and methionine and residual trypsin inhibitors, and through a biological evaluation of protein digestibility and quality. Both pressure cooking products had similar functional and chemical characteristics, however, the 5-minute cooked product has higher protein quality than the 10-minute product.(ABSTRACT TRUNCATED AT 250 WORDS)

Fabaceae↗

PubMed1993

Characterization of PEA-15, a major substrate for protein kinase C in astrocytes.

Astrocytes in the central nervous system are involved in a variety of functions including storage of glycogen, maintenance of the extracellular ionic equilibrium, and support for the migration and the differentiation of neurons. Astrocytes express membrane receptors allowing them to respond to extracellular signals. Activation of receptors induces a cascade of events, such as stimulation of protein kinases and subsequent phosphorylation of target proteins. To understand the regulatory processes underlying neuroglial interactions, attempts were made to identify major phosphorylated proteins in striatal astrocytes, grown in primary culture and labeled with [32P]phosphate. Two-dimensional gel electrophoresis revealed a major doublet, Pa and Pb, of highly labeled spots, with a low molecular weight (M(r) = 15,000) and acidic pI (pI = 5.2 and 5.3, respectively). Using an enriched, heat-stable, cytosolic fraction, Pa and Pb were eluted from semi-preparative two-dimensional gels and subjected to a limited proteolysis and partial microsequencing. The same sequences were obtained within Pa and Pb and had no homology with other known protein. Antibodies raised against corresponding synthetic peptides confirm that the doublet represents two isoelectric variants of the same protein, which also exists under a nonphosphorylated form, N. We propose to name this protein PEA-15, for Phosphoprotein Enriched in Astrocytes-15 kDa, according to its large enrichment in these cells. Treatment of intact astrocytes with 12-O-tetradecanoylphorbol-13-acetate (TPA), which stimulates protein kinase C (PKC), increased the phosphorylation of the more acidic spot (Pb) while decreasing Pa intensity. Stimulations of astrocytes known to increase PKC activity, i.e. noradrenaline, or its inhibition by decreasing extracellular calcium concentrations, staurosporine, or desensitization following long term treatment with TPA, induced a phosphorylation or a dephosphorylation of PEA-15, respectively. Using purified PKC, PEA-15 appeared to be a good substrate in vitro. Two-dimensional peptide mapping revealed that the phosphorylation site in intact cells was identical with the site phosphorylated by PKC in vitro. Mapping the phosphopeptides by HPLC following endolysine C treatment lead to the identification of a sequence, phosphorylated in intact astrocytes and in vitro by PKC, containing a consensus site for PKC: LTRIPSAKK. Antibodies raised against a synthetic peptide derived from this sequence recognized N and Pa in control conditions and Pb after its dephosphorylation. Thus, PEA-15 is an endogenous substrate for PKC, the kinase mediating the transition from Pa to Pb.

Amino Acid Sequence↗