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 Amino Acid Sequence of the Smaller Subunit of Conglutin ?, a Storage Globulin of Lupinus angustifolius

1977 ◽  
Vol 30 (2) ◽  
pp. 33 ◽  
Author(s):  
TC Elleman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Storage Protein ◽  
Storage Proteins ◽  
Lupinus Angustifolius ◽  
Amino Acid Residues ◽  
A Subunit

The amino acid sequence of the smaller subunit of conglutin y, the simplest of the three globulins from the seeds of Lupinus angusti/olius cv. Uniwhite, has been determined. The subunit was homogeneous and contained 154 amino acid residues, including five sulphur-containing amino acids-a considerably higher content than is found in most other legume storage proteins. There was no indication of the complexity experienced in studies of many other legume storage proteins. This is perhaps the first sequence of a subunit of a legume storage protein to be determined.

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 Proteome Map of Pea (Pisum Sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls

2018 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Pea Seed

Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major economically important legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Obviously, changes in seed protein patterns might directly affect both of these aspects. Thus, here we address the pea seed proteome in more detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. Accordingly, 1938 and 1989 non-redundant proteins were identified in yellow and green pea seeds, in total. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP) potentially indicating the high efficiency of our experimental workflow. In total 981 protein groups could be assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.

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.

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