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At least 829 records · Page 46Linked to original sources
PubMed1992

Rapid alterations in growth rate and electrical potentials upon stem excision in pea seedlings.

Excision of the epicotyl base of pea (Pisum sativum L.) seedlings in air results in a fast drop in the growth rate and rapid transient membrane depolarization of the surface cells near the cut. Subsequent immersion of the cut end into solution leads to a rapid, transient rise in the epicotyl growth rate and an acropetally propagating depolarization with an amplitude of about 35 mV and a speed of approx. 1 mm s-1. The same result can be achieved directly by excision of the pea epicotyl under water. Shape, amplitude and velocity of the depolarization characterize it as a "slow-wave potential". These results indicate that the propagating depolarization is caused by a surge in water uptake. Neither a second surge in water uptake (measured as a rapid increase in growth rate when the cut end was placed in air and then back into solution) nor another cut can produce the depolarization a second time. Cyanide suppresses the electrical signal at the treated position without inhibiting its transmission through this area and its development in untreated parts of the epicotyl. The large depolarization and repolarization which occur in the epidermal and subepidermal cells are not associated with changes in cell input resistance. Both results indicate that it is a transient shut-down of the plasma-membrane proton pump rather than large ion fluxes which is causing the depolarization. We conclude that the slow wave potential is spread in the stem via a hydraulic surge occurring upon relief of the negative xylem pressure after the hydraulic resistance of the root has been removed by excision.

Membrane Potentials↗
PubMed1993

The organisation and expression of the genes encoding the mitochondrial glycine decarboxylase complex and serine hydroxymethyltransferase in pea (Pisum sativum).

Restriction fragment length polymorphisms have been used to determine the chromosomal location of the genes encoding the glycine decarboxylase complex (GDC) and serine hydroxymethyltransferase (SHMT) of pea leaf mitochondria. The genes encoding the H subunit of GDC and the genes encoding SHMT both show linkage to the classical group I marker i. In addition, the genes for the P protein of GDC show linkage to the classic group I marker a. The genes for the L and T proteins of GDC are linked to one another and are probably situated on the satellite of chromosome 7. The mRNAs encoding the five polypeptides that make up GDC and SHMT are strongly induced when dark-grown etiolated pea seedlings are placed in the light. Similarly, when mature plants are placed in the dark for 48 h, the levels of both GDC protein and SHMT mRNAs decline dramatically and then are induced strongly when these plants are returned to the light. During both treatments a similar pattern of mRNA induction is observed, with the mRNA encoding the P protein of GDC being the most rapidly induced and the mRNA for the H protein the slowest. Whereas during the greening of etiolated seedlings the polypeptides of GDC and SHMT show patterns of accumulation similar to those of the corresponding mRNAs, very little change in the level of the polypeptides is seen when mature plants are placed in the dark and then re-exposed to the light.

Amino Acid Oxidoreductases↗
PubMed1994

Two distinct cis-acting elements are involved in light-dependent activation of the pea elip promoter.

Light activation of the pea (Pisum sativum) elip gene promoter was analysed in transgenic plants and in transiently transfected plant protoplasts. A series of promoter deletions fused to the gusA reporter was tested, and the results obtained by the two experimental approaches were in good agreement. We identified two nucleotide sequence elements involved in light-regulated expression of the elip gene. One element is similar to the GT1 binding site of the rbcS-3A gene, and the other resembles a G-box-like ACGT element. The region containing both elements was able to confer light responsiveness on a heterologous basic promoter. Electrophoretic mobility shift assays demonstrated that each element is specifically recognized by DNA-binding proteins present in nuclear extracts from pea seedlings. The G-box-like ACGT element is necessary but not sufficient for light inducibility, indicating that the two elements act together in confering light responsiveness.

Arabidopsis Proteins↗
PubMed1991

Sequence and transcriptional analysis of the gene cluster trnQ-zfpA-psaI-ORF231-petA in pea chloroplasts.

A 5.1 kb segment of pea chloroplast DNA containing the upstream region of petA was sequenced. RNAs produced from this DNA were characterized. This region encodes putative genes for psbK, trnQ, zfpA, psaI, ORF231, and petA. These genes are all on the same reading strand except for psbK. The gene organization is somewhat different from that of tobacco, rice, and liverwort, which lack the psbK-trnQ genes in this region and contain ORF184/185. Northern blot and primer extension analysis show that the pea transcript covers the zfpA-psaI-ORF231-petA gene cluster and trnQ. These results indicated that the psbK-trnQ genes have been rearranged and a new transcription unit was formed.

Amino Acid Sequence↗
PubMed1987

The structure and light-dependent transient expression of a nuclear-encoded chloroplast protein gene from pea (Pisum sativum L.).

A nuclear gene encoding a light-induced transiently expressed protein that is localized in the chloroplast has been isolated from an EMBL3 library of pea DNA. The gene is a member of a multigene family. The sequence of the gene contains the complete reading frame of previously characterized cDNA clones and two introns in the 5' region of the protein coding sequence. Primer extension and S1 nuclease studies have defined the cap site. Two TATA boxes are found 5' to the initiating methionine codon. Only a limited homology is found between the presequence of the gene and transit sequences of other previously sequenced precursors. Isolated nuclei of pea have been labelled and the in vitro synthesized transcripts analysed. The results show that the light-dependent expression of the gene family is regulated at the level of transcription.

Amino Acid Sequence↗
PubMed1988

Analysis of pss genes of Rhizobium leguminosarum required for exopolysaccharide synthesis and nodulation of peas: their primary structure and their interaction with psi and other nodulation genes.

Strains of Rhizobium leguminosarum (R.l.) biovar viciae containing pss mutations fail to make the acidic exopolysaccharides (EPS) and are unable to nodulate peas. It was found that they also failed to nodulate Vicia hirsuta, another host of this biovar. When peas were co-inoculated with pss mutant derivatives of a strain of R.l. by viciae containing a sym plasmid plus a cured strain lacking a sym plasmid (and which is thus Nod-, but for different reasons) but which makes the acidic EPS, normal numbers of nodules were formed, the majority of which failed to fix nitrogen (the occasional Fix+ nodules were presumably induced by strains that arose as a result of genetic exchange between cells of the two inoculants in the rhizosphere). Bacteria from the Fix- nodules contained, exclusively, the strain lacking its sym plasmid. When pss mutant strains were co-inoculated with a Nod- strain with a mutation in the regulatory gene nodD (which is on the sym plasmid pRL1JI), normal numbers of Fix+ nodules were formed, all of which were occupied solely by the nodD mutant strain. Since a mutation in nodD abolishes activation of other nod genes required for early stages of infection, these nod genes appear to be dispensable for subsequent stages in nodule development. Recombinant plasmids, containing cloned pss genes, overcame the inhibitory effects of psi, a gene which when cloned in the plasmid vector pKT230, inhibits both EPS production and nodulation ability. Determination of the sequence of the pss DNA showed that one, or perhaps two, genes are required for correcting strains that either carry pss mutations or contain multi-copy psi.(ABSTRACT TRUNCATED AT 250 WORDS)

Bacterial Proteins↗
PubMed1989

Sequences responsible for the tissue specific promoter activity of a pea legumin gene in tobacco.

Maturing pea cotyledons accumulate large quantities of storage proteins at a specific time in seed development. To examine the sequences responsible for this regulated expression, a series of deletion mutants of the legA major seed storage protein gene were made and transferred to tobacco using the Bin19 disarmed Agrobacterium vector system. A promoter sequence of 97 bp including the CAAT and TATA boxes was insufficient for expression. Expression was first detected in a construct with 549 bp of upstream flanking sequence which contained the the leg box element, a 28 bp conserved sequence found in the legumin-type genes of several legume species. Constructs containing -833 and -1203 bp of promoter sequence significantly increased levels of expression. All expressing constructs preserved seed specificity and temporal regulation. The results indicate that promoter sequences between positions -97 and -549 bp are responsible for promoter activity, seed specificity, and temporal regulation of the pea legA gene. Sequences between positions -549 and -1203 bp appear to function as enhancer-like elements, to increase expression.

Base Sequence↗
PubMed1986

Enzymatic control of anthocyanin expression in the flowers of pea (Pisum sativum) mutants.

Using enzymological and immunological methods we have investigated the relationship between chalcone synthase and the A locus, a major gene involved in the control of anthocyanin expression in pea (Pisum sativum L.) flowers. Pea plants containing the dominant allele A usually synthesize anthocyanins in the petal tissue, whereas plants homozygous for the a allele do not produce anthocyanins. We sought to determine whether or not the A locus also controlled the presence or absence of chalcone synthase, the first enzyme of the flavonoid pathway in the flowers of three genetic lines (A, purple-violet flowers; A,am, white flowers with sometimes pink edges; and a, white flowers). Chalcone synthase was found to be present in all three genetic lines by enzyme activity measurement, indirect enzyme-linked immunosorbent assay (ELISA), and Western blotting. Spectroscopic investigations showed that only the genetic lines A and A,am contained anthocyanins and flavonol glycosides, respectively, in the flowers; line a accumulated p-coumaric acid or its derivatives. These data suggest that the A locus in Pisum is not the structural gene for chalcone synthase and it does not appear to regulate the expression of this enzyme.

Acyltransferases↗
PubMed1997

Purification, characterization and physiological role of sucrose synthase in the pea seed coat (Pisum sativum L.).

The seed coat is a maternal organ which surrounds the embryo and is involved in the control of its nutrition. This study with pea (Pisum sativum L.) was conducted to understand more fully the sucrose/starch interconversions occurring in the seed coat. The concentrations of soluble sugars, the starch content, and the activities of the sucrose-metabolizing enzymes, sucrose synthase (Sus; EC 2.4.1.13), alkaline and soluble acid invertase (EC 3.2.1.26) and sucrose-phosphate synthase (SPS; EC 2.4.1.14) were compared at four developmental stages during seed filling. Among the four enzymes, only Sus activity was very high and strongly correlated with the starch concentration in the seed coat. Sucrose synthase catalyses the cleavage of sucrose in the presence of UDP into UDP-glucose and fructose. Sucrose synthase was purified from pea seed coats in a three-step protocol, consisting of diethylaminoethyl-Sephacel chromatography, gel filtration and affinity chromatography. The enzyme was characterized at the biochemical and molecular levels. Sucrose synthase exhibits biochemical properties which allow it to function in the direction of both sucrose cleavage and synthesis. The mass-action ratio of its four substrate was close to the theoretical equilibrium constant at the four developmental stages we studied. A labelling experiment on seed coats has shown that Sus activity is reversible in vivo and can produce 37% of neo-synthesized sucrose in the seed coat cells (minimum value). It is concluded that Sus could play a central role in the control of sucrose concentration in the seed coat cells in response to the demand for sucrose in the embryo during the development of the seed.

Base Sequence↗
PubMed1994

Biological utilization of vegetable peas: effect of cooking and varietal differences.

The flour of raw as well as cooked vegetable pea cultivars (Arkal and Bonneville) was used for biological evaluation of their protein quality. Cooking did not have a significant influence on the food intake. There were some differences in the food as well as protein intake and gain in body weights of rats when fed uncooked or cooked pea flour diets. Varietal differences did not seem to influence on apparent digestibility, true digestibility, biological value, net protein utilization and utilisable protein but cooking brought a significant (p < 0.05) improvement in all of above mentioned parameters. Varietal differences as well as cooking exhibited no influence or serum protein concentration.

Animals↗
PubMed1994

Effect of heat treatment and germination on alpha amylase inhibitor activity in chick peas (Cicer arietinum L.).

Chick pea seeds of twenty eight varieties were analysed for alpha amylase inhibitor activity (AIA) using salivary amylase. The effects of heat treatment and germination on the activity of the antinutritional factor was investigated. Heat treatment and germination decreased the activity of amylase inhibitor. Chick pea meal was also subjected to UV irradiation and pressure cooking. These treatments decreased alpha amylase inhibitor activity. The amylase inhibitor activity decreased as the days of germination increased and negligible inhibitor activity was observed on the 6th day of germination.

Cooking↗
PubMed1996

Biological and chemical evaluation of chick pea seed proteins as affected by germination, extraction and alpha-amylase treatment.

The effects of germination, extraction (double extraction with 70% ethanol and water at isoelectric point) and alpha-amylase treatments of chick pea seed flours on crude protein, total carbohydrate, protein efficiency ratio (PER), biological value (BV), true digestibility (TD), net protein utilization (NPU), essential amino acid composition, in-vitro protein digestibility (IVPD) and actual amino acid indices (essential amino acid index or amino acid score) were evaluated. Crude protein content was increased (8-149%), while total carbohydrate was decreased (11-62%) by germination, extraction and alpha-amylase treatments. Alpha-amylase treatment was more efficient in reducing total carbohydrate and increasing the protein content than that of extraction treatment. The protein quality of chick pea flours as measured by PER, BV, TD, NPU, IVPD and corrected amino acid indices (actual amino acid indices x IVPD) was significantly improved by these treatments. The protein quality of germinated-alpha-amylase treatment was comparable with casein, while germinated-alpha-amylase treaded seeds appeared nutritionally superior to casein. The results indicate that the germinated-alpha-amylase and germinated-alpha-amylase-extracted treatments could be used successfully as a source of concentrated high quality protein for baby food production. The corrected amino acid indices gave better prediction of PER, BV, TD and NPU (r = 93 to 97) than actual amino acid indices (r = 45 to 71). PER was highly correlated with corrected amino acid score (r = 0.93). The PER could be predicted from the following simple regression equation: PER = -1.827 + 0.0561 x corrected amino acid score.

Dietary Proteins↗
PubMed1996

A preliminary study on the effect of germination on saponin content and composition of lentils and chick peas.

Two cultivars of chick peas (Cicer arietinum) and one cultivar of lentils (Lens culinaris) were subjected to germination in the dark for 6 days at 20 degrees C. Soyasaponin VI, also known as soyasaponin beta g, a DDMP- (2,3-dihydro-2,5-dihydroxy-6-methyl-4H-pyran-4-one-) conjugated form of soyasaponin I, was the only saponin detected in both the unprocessed and germinated seed. No significant changes in saponin content were observed for chick peas or lentils after a 6-day germination.

Carbohydrate Sequence↗
PubMed1986

Lectin-resistant CHO cells: selection of four new pea lectin-resistant phenotypes.

The cytotoxic plant lectins from P. sativum have been used to select new lectin-resistant mutants from Chinese hamster ovary (CHO) cells. Two novel phenotypes that behave recessively but fall into the same complementation group have been termed Lec13 and Lec13A. Both of these mutant types are phenotypically reverted to pea lectin sensitivity following growth in L-fucose. In contrast, two other unique phenotypes behave dominantly in somatic cell hybrids and maintain their pea lectin-resistance in the presence of L-fucose. They have been termed LEC14 and LEC18, respectively. The lectin-resistance and complementation properties of the four new mutant types suggest that they define three different glycosylation genes of the CHO genome.

Animals↗
PubMed1993

Changes in some constituents of pea seed during commercial canning.

Changes in crude protein (CP), non protein nitrogen (NPN), total sulphur (TS) contents, carbon/nitrogen (C/N) and nitrogen/sulphur (N/S) ratios and albumin protein (AP) were studied in four sizes of peas at various stages of the commercial canning process. Of all the parameters considered, NPN, AP, and TS showed the most regular trend to decrease during the commercial canning process. In this paper the use of these three parameters is proposed to obtain a Heat Treatment Index (HTI) applicable to raw, blanched and canned peas, according to the equation: HTI = (NPN x AP)/TS.

Albumins↗
PubMed1981

Unsaponifiable matter and fatty acid composition of pea oil.

14 compounds were detected in the unsaponifiable matter of pea oil by gas liquid chromatography (GLC) and 8 of them were identified as hydrocarbons C30, C32, squalene, alpha-tocopherol, cholesterol, campesterol, stigmasterol and beta-sitosterol. The predominant unsaponifiable fraction was beta-sitosterol whereas the others were found in variable amounts. Two sterols were isolated by column chromatography. One of them was characterised as beta-sitosterol by measuring the melting point, [a]D, and infrared spectra and those of its acetate. However, the other sterol was unidentified. The fatty acid contents in pea oil were determined quantitatively by GLC. They were present in variable amounts, whereas linoleic acid was the major one.

Chromatography, Gas↗
PubMed1996

Correlation of nonanucleotide motifs with transcript initiation of 18S rRNA genes in mitochondria of pea, potato and Arabidopsis.

Transcription initiation sites for the mitochondrial 18S rRNA genes in the dicot plants Arabidopsis thaliana, potato and pea were identified by a combination of in vitro capping, primer extension and S-1 analyses. These promoters contain a nonanucleotide motif and an AT-rich sequence similar to many mRNA and tRNA promoters in dicot mitochondria. In Arabidopsis and potato, active promoters are located within 120 nucleotides upstream of the 18S rRNA genes, as in Oenothera. The nucleotide sequence in the corresponding region in pea mitochondria is well conserved, but is not used as promoter in this plant. Instead a novel promoter sequence is used that lies several hundred nucleotides upstream. These results show that rRNAs can be transcribed from the same promoter types as mRNAs and tRNAs in plant mitochondria. However, the sequence features presently attributed to plant mitochondrial promoters-the conserved nonanucleotide and the upstream AT-rich box-do not allow to deduce the presence of an active promoter from genomic sequence data alone.

Arabidopsis↗
PubMed1998

Half-embryo cocultivation technique for estimating the susceptibility of pea (Pisum sativum L.) and lentil (Lens culinaris Medik.) cultivars to Agrobacterium tumefaciens.

Longitudinally sliced embryonic axes from pea and lentil mature seeds cocultivated with A. tumefaciens carrying a gus reporter gene in its T-DNA provided a convenient means to evaluate the efficiency of gene transfer to tissues in different cultivars and cocultivation conditions. Use of this technique demonstrated wide variation in susceptibility to Agrobacterium among several pea and lentil commercial genotypes.

Agrobacterium tumefaciens↗