Cotyledonary Storage Proteins in Pisum Sativum. II. Hereditary Variation in Components of the Legumin and Vicilin Fractions

1978 ◽  
Vol 5 (3) ◽  
pp. 281 ◽  
Author(s):  
JA Thomson ◽  
HE Schroeder
Keyword(s):  
Pisum Sativum ◽  
Phenotypic Variation ◽  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Gene Products ◽  
Hereditary Variation ◽  
Pea Seeds ◽  
Parental Lines ◽  
Variant System

Gel electrophoresis has been used to investigate genetically controlled variation in storage-protein constituents forming five series of bands (LA-LE) derived from legumin fractions, and three series of bands (VA-VC) from vicilin fractions, of pea seeds. In each variant system, the phenotypes of the storage-protein polypeptides from F1 seeds were additive with respect to the band patterns of the parental lines, and identical in reciprocal crosses. Neither dominance nor formation of new interaction products was observed. Variation in the three systems involving vicilin polypeptides and two of those involving legumin components was found to be based on allelic alternatives at single loci designated Vicilin A (Vca), Vicilin B (Vcb), Vicilin C (Vcc), Legumin A (Lga) and Legumin C (Lgc). For each of these variant systems, the gene products involved and the basis of the phenotypic variation have been discussed. Variants of the VC band complex, in which mobility of two bands both composed of 12 and 14 kdalton polypeptides is altered, appear likely to correspond to vicilin variants described previously. Type lines are specified for each of the variant phenotypes analysed, and for the genes designated.

scholarly journals Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea (Pisum sativum L.)

1985 ◽  
Vol 225 (1) ◽  
pp. 239-247 ◽  
Author(s):  
J A Gatehouse ◽  
J Gilroy ◽  
M S Hoque ◽  
R R D Croy
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Amino Acid Sequence ◽  
Storage Protein ◽  
Seed Protein ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Pisum Sativum L ◽  
New Type ◽  
Pea Seeds

The seeds of pea (Pisum sativum L.) contain several proteins in the albumin solubility fraction that are significant components of total cotyledonary protein (5-10%) and are accumulated in developing seeds concurrently with storage-protein synthesis. One of these proteins, of low Mr and designated ‘Psa LA’, has been purified, characterized and sequenced. Psa LA has an Mr of 11000 and contains polypeptides of Mr 6000, suggesting that the protein molecules are dimeric. The amino acid sequence contains 54 residues, with a high content (10/54) of asparagine/aspartate. It has no inhibitory action towards trypsin or chymotrypsin, and is distinct from the inhibitors of those enzymes found in pea seeds, nor does it inhibit hog pancreatic alpha-amylase. The protein contains no methionine, but significant amounts of cysteine (four residues per polypeptide), suggesting a possible role as a sulphur storage protein. However, its sequence is not homologous with low-Mr (2S) storage proteins from castor bean (Ricinus communis) or rape (Brassica napus). Psa LA therefore represents a new type of low-Mr seed protein.

scholarly journals Genetically Controlled Electrophoretic Variants of a Storage Protein in Pisum Sativum

1968 ◽  
Vol 21 (4) ◽  
pp. 827 ◽  
Author(s):  
MJ Hynes
Keyword(s):  
Pisum Sativum ◽  
Genetic Control ◽  
Storage Protein ◽  
Storage Proteins ◽  
Genetic Studies ◽  
Electrophoretic Variants ◽  
Electrophoretic Patterns ◽  
Wheat Storage Proteins ◽  
And Storage

A number of electrophoretic variants of plant enzymes have been described and the genetic control of these variants determined (e.g. Beckman, Scandalios, and Brewbaker 1964; Schwartz 1964; Scandalios 1965). However, little work has been done on structural and storage proteins of plants. Varietal differences have been observed in the electrophoretic patterns of wheat storage proteins (Graham and Morton 1963) and two forms of arachin, a storage protein of the peanut, have been described (Tombs 1964), though no genetic studies of these differences have been made. This communication describes the detection and the partial characterization of variants of proteins extracted from the cotyledons of Pisum sativum seeds and some preliminary breeding tests to determine their genetic control.

Profiling the Seed Storage Protein Among Different Genotypes of Trigonella foenum-graecum L. (Fenugreek)

2019 ◽  
Author(s):  
Nisha . ◽  
Priyanka Khati ◽  
P B Rao
Keyword(s):  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Band ◽  
Trigonella Foenum Graecum ◽  
Trigonella Foenum Graecum L

A qualitative as well as quantitative categorization of seed storage proteins profiles of 23 genotypes of Trigonella foenum- graecum L. were performed by using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) for exploring the level of genetic discrepancy at seed storage protein level. Total soluble proteins were resolved on 10% resolving gel. A dendrogram was constructed on the basis of weight of seed storage proteins, which divide total genotypes into two groups further classified into different sub groups containing different genotypes in them. The bands obtained from gel electrophoresis can serve as a potent tool in discrimination of different genotypes on the basis of their protein content. Proteins with molecular weight 66, 43 and 35 kDa were found in all the genotypes except Fgk-76, PR, Rmt-303, PEB and Rmt-361, The 43 kDa protein band was found missing in Fgk-67, AFg-2, AM-2, AFg-4, Fgk-73, although the protein with 35 kDa weight was present in all the genotypes but not in Rmt-303 same as 63 kDa which is not present in Fgk-70 and 55 kDa protein band was found missing in Fgk-67, Afg-4 and Rmt-361.

scholarly journals The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)

1980 ◽  
Vol 191 (2) ◽  
pp. 509-516 ◽  
Author(s):  
R R Croy ◽  
J A Gatehouse ◽  
M Tyler ◽  
D Boulter
Keyword(s):  
Genetic Variation ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Purification And Characterization ◽  
Native Form ◽  
Pisum Sativum L ◽  
A Subunit ◽  
Cnbr Cleavage ◽  
Pea Seeds

A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named ‘convicilin’ and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.

Cotyledonary Storage Proteins in Pisum sativum. I. Molecular Heterogeneity

1978 ◽  
Vol 5 (3) ◽  
pp. 263 ◽  
Author(s):  
JA Thomson ◽  
HE Schroeder ◽  
WF Dudman
Keyword(s):  
Cellulose Acetate ◽  
Electrophoretic Mobility ◽  
Storage Protein ◽  
Storage Proteins ◽  
Electrophoretic Analysis ◽  
Molecular Heterogeneity ◽  
Polypeptide Composition ◽  
Ph Values ◽  
Pea Seeds ◽  
Differential Solubility

The two storage-protein fractions of pea seeds, legumin and vicilin, have each been resolved electrophoretically on a cellulose acetate gel matrix into multiple molecular species distinguished by electrophoretic mobility and by quantitative or qualitative differences in subunit composition or both. Electrophoretograms of these apparent holoproteins from a range of lines and cultivars were found to be genotype-specific, generally showing three strong bands, together with up to three additional minor bands, assignable to a vicilin series of components. A further three or four bands could be assigned to a legumin series, although the slowest of these showed apparent admixture of certain polypeptides typical of the vicilin fractions. Each putative holoprotein band in both the legumin and vicilin series behaved additively in the electrophoretograms of F1 offspring from reciprocal crosses between lines showing distinct patterns. For comparison with the proteins distinguished electrophoretically on cellulose acetate gels, storage proteins from lyophilized protein bodies were fractionated on the basis of differential solubility at various ionic strengths and pH values. The single legumin and three vicilin fractions obtained by this method showed sedimentation velocities typical of the respective holoproteins. No overlap in the polypeptide composition of legumin with that of vicilin fractions was observed. The components represented in the four fractions accounted for all the major polypeptides in total storage-protein extracts and in the bands eluted from cellulose acetate gels. The distinctive polypeptide pattern and electrophoretic mobility of vicilin fraction 4 identified this protein as a contaminant of slow legumin bands in cellulose acetate gels, and as an additional vicilin species not recognized directly from the electrophoretic analysis.

The genetics of legume storage proteins

1984 ◽  
Vol 304 (1120) ◽  
pp. 349-358 ◽  
Keyword(s):  
Phaseolus Vulgaris ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Mendelian Inheritance ◽  
French Bean ◽  
Messenger Rnas ◽  
Polypeptide Structure

The seed storage proteins of Pisum (pea) and Phaseolus vulgaris (French bean) exhibit genetic variation for polypeptide structure; genetical studies indicate that most of the major storage protein genes exhibit simple, codominant Mendelian inheritance. Biochemical analysis of the storage protein polypeptides and their messenger RNAs shows that the allelic alternatives are probably small families of closely linked structural genes. Two of these genes - those for the major legumin gene family and for convicilin, both from Pisum sativum - have been assigned to specific sites on linkage groups. Genes affecting the synthesis of legumin in Pisum sativum and of phaseolin in Phaseolus vulgaris have been identified.

The microbial community associated with pea seeds (Pisum sativum) of different geographical origins

2021 ◽  
Author(s):  
Valentine Chartrel ◽  
Eric Dugat-Bony ◽  
Anne-Sophie Sarthou ◽  
Sophie Huchette ◽  
Pascal Bonnarme ◽  
...  
Keyword(s):  
Microbial Community ◽  
Pisum Sativum ◽  
Pea Seeds

β-Amyrin Synthase1 Controls the Accumulation of the Major Saponins Present in Pea (Pisum sativum)

2021 ◽  
Author(s):  
Vanessa Vernoud ◽  
Ludivine Lebeigle ◽  
Jocelyn Munier ◽  
Julie Marais ◽  
Myriam Sanchez ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Bitter Taste ◽  
Crop Improvement ◽  
Functional Protein ◽  
Saponin Biosynthesis ◽  
Physiological Quality ◽  
Pea Seeds ◽  
Identification And Characterization ◽  
Pea Seed

Abstract The use of pulses as ingredients for the production of food products rich in plant proteins is increasing. However, protein fractions prepared from pea or other pulses contain significant amounts of saponins, glycosylated triterpenes which can impart an undesirable bitter taste when used as an ingredient in foodstuffs. In this paper, we describe the identification and characterization of a gene involved in saponin biosynthesis during pea seed development, by screening mutants obtained from two Pisum sativum TILLING (Targeting Induced Local Lesions in Genomes) populations in two different genetic backgrounds. The mutations studied are located in a gene designated PsBAS1 (β-amyrin synthase1) which is highly expressed in maturing pea seeds and which encodes a protein previously shown to correspond to an active β-amyrin synthase. The first allele is a nonsense mutation, while the second mutation is located in a splice site and gives rise to a mis-spliced transcript encoding a truncated, non-functional protein. The homozygous mutant seeds accumulated virtually no saponin without affecting seed nutritional or physiological quality. Interestingly, BAS1 appears to control saponin accumulation in all other tissues of the plant examined. These lines represent a first step in the development of pea varieties lacking bitterness off-flavours in their seeds. Our work also shows that TILLING populations in different genetic backgrounds represent valuable genetic resources for both crop improvement and functional genomics.

Proximate and mineral composition of field peas

1997 ◽  
Vol 77 (1) ◽  
pp. 101-103 ◽  
Author(s):  
T. D. Warkentin ◽  
A. G. Sloan ◽  
S. T. Ali-Khan
Keyword(s):  
Pisum Sativum ◽  
Key Words ◽  
Mineral Composition ◽  
Seed Yield ◽  
Total Protein ◽  
Field Pea ◽  
Pisum Sativum L ◽  
Field Peas ◽  
Pea Seeds ◽  
Proximate And Mineral Composition

Field pea seeds from 10 cultivars grown at two locations in Manitoba in 1986 and 1987 were analyzed for proximate and mineral profiles. Cultivars differed significantly in their level of total protein, crude fat, ADF, and all minerals tested. However, differences were not extremely large and were comparable to European reports. Location-year also had a significant effect on the levels of total protein, ADF, and all minerals tested. In most cases, the warmest location-year produced relatively higher levels of minerals, ash, and total protein, and lower seed yield than the coolest location-year. Key words: Field pea, Pisum sativum L., mineral

scholarly journals Reciprocal effect of parental lines on the physiological potential and seed composition of corn hybrid seeds

2017 ◽  
Vol 27 (3) ◽  
pp. 206-216 ◽  
Author(s):  
Juliana F. Santos ◽  
Lynnette M.A. Dirk ◽  
A. Bruce Downie ◽  
Mauricio F.G. Sanches ◽  
Roberval D. Vieira
Keyword(s):  
Storage Proteins ◽  
Soluble Sugar ◽  
Soluble Sugars ◽  
Major Protein ◽  
Seed Composition ◽  
Seed Vigour ◽  
Reciprocal Crosses ◽  
Hybrid Seeds ◽  
Parental Lines ◽  
Corn Hybrid

AbstractObtaining corn hybrid seeds (Zea mays L.) with high vigour depends on the parental lines and the direction of the cross, and this relates to seed desiccation tolerance and composition. This research studied reciprocal crosses between pairs of proprietary, elite parent lines (L1 and L5; L2 and L4) producing hybrid seeds with different qualities attempting to correlate vigour with seed composition, focusing on storage proteins, starch and soluble sugar amounts. Four corn hybrid seed lots produced from reciprocal crosses were compared (HS 15 with HS 51, and HS 24 with HS 42) by assessing germination, vigour, and seedling emergence in the field. Seed composition was assessed in mature, dehydrated seeds. Proteins were extracted, quantified, and analysed by electrophoresis and densitometry. Starch amounts were assessed using a kit and soluble sugars were determined using high performance liquid chromatography with pulsed electrochemical detection. The L1 and L2 lineages, used as female parents, provided seeds with lower vigour; however, the quantification of major protein bands, and sucrose, raffinose and stachyose were similar between seed lot pairs. While both total seed protein and starch varied between reciprocal hybrids for one of the two sets of crosses, the amounts of neither correlated with seed vigour. Interestingly, hybrids with low seed vigour (HS 15, HS 24) accumulated greater amounts of fructose relative to their reciprocal; correlation analysis confirmed these results. We demonstrate different effects on seed vigour dependent on the maternal parent in reciprocal crosses producing hybrid corn seeds. We also show that vigour is negatively correlated with seed reducing sugar contents.

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