scholarly journals Convicilin mRNA from pea (Pisum sativum L.) has sequence homology with other legume 7S storage protein mRNA species

1984 ◽  
Vol 224 (2) ◽  
pp. 661-666 ◽  
Author(s):  
R Casey ◽  
C Domoney ◽  
J Stanley
Keyword(s):  
Nucleotide Sequence ◽  
Pisum Sativum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nucleotide Sequence Analysis ◽  
Sequence Difference ◽  
Legume Seed ◽  
Complementary Dna ◽  
Pisum Sativum L

Nucleotide-sequence analysis of a complementary-DNA clone for convicilin, one of the storage proteins from pea (Pisum sativum L.) seeds, shows it to be homologous with the 7S legume seed storage proteins vicilin, conglycinin and phaseolin. Convicilin is more similar to vicilin than to phaseolin or to conglycinin. Significant areas of sequence difference are discussed.

scholarly journals The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.)

1982 ◽  
Vol 207 (3) ◽  
pp. 629-632 ◽  
Author(s):  
J A Gatehouse ◽  
G W Lycett ◽  
R R D Croy ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Pisum Sativum ◽  
Tryptic Peptide ◽  
Proteolytic Cleavage ◽  
Amino Acid Sequencing ◽  
Complementary Dna ◽  
Pisum Sativum L ◽  
Peptide Profiles

Tryptic-peptide profiles and amino acid sequencing of purified pea (Pisum sativum L.) vicilin subunits were used to show that their sequences were interrelated. Comparison with the nucleotide sequence of a cloned vicilin complementary DNA (mRNA) showed that all vicilin subunits could be derived from 50 000-Mr precursors containing up to two sites for post-translational proteolytic cleavage, and allowed these subunits to be located relative to the precursor.

Calcium- and Magnesium-Dependent Aggregation of Legume Seed Storage Proteins

1999 ◽  
Vol 47 (8) ◽  
pp. 3009-3015 ◽  
Author(s):  
Ricardo B. Ferreira ◽  
Emanuel Franco ◽  
Artur R. Teixeira
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Legume Seed ◽  
Calcium And Magnesium

Electrophoretic and immunochemical techniques for the molecular reassessment of relationships within Vicieae

2007 ◽  
Vol 55 (2) ◽  
pp. 131-147
Author(s):  
R. Sammour
Keyword(s):  
Pisum Sativum ◽  
Vicia Faba ◽  
Cicer Arietinum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Immunochemical Study ◽  
Partial Identity ◽  
Electrophoretic Patterns ◽  
Immunochemical Techniques

In this study, an array of electrophoretic and immunochemical techniques was used to investigate the legumins, vicilins and albumins of seed storage proteins in Pisum sativum , Vicia faba , Lens esculentum , and Cicer arietinum to delimit the boundary of the tribe Vicieae and to clarify the systematic position of the genus Cicer . The band patterns of the legumins of these species were broadly similar in that they had bands at Mr 60 kDa which disappeared in the presence of 2-mercaptoethanol, giving rise to two sets of new bands, at Mr approximately 40 kDa and 20 kDa, representing acidic or α and basic or β subunits. The band patterns of the vicilins were also quite similar in that they showed bands at Mr approximately 71 kDa (convicilin) and 50 kDa (vicilin), which were not altered by the presence of 2-mercaptoethanol. Serologically, the legumins of Vicia faba and Lens esculentum exhibited total identity with Pisum legumin antiserum under nonreducing conditions, whereas the legumin of Cicer arietinum exhibited only partial identity, which was attributed to the failure of the low molecular subunit pair (Mr 33 kDa) to react with Pisum legumin antiserum. On the other hand, the vicilins of Vicia faba , Lens esculentum and Cicer arietinum had only partial identity with the vicilin of Pisum sativum , which was due to the failure of a number of subunits along the electrophoretic patterns of these species to react with Pisum sativum vicilin antiserum. The electrophoretic patterns of Vicia faba , Lens esculentum and Cicer arietinum were markedly different for the albumins. However, immunochemically they gave a positive reaction with Pisum major albumin antiserum (Mr 25 kDa) and showed a band with a molecular weight slightly higher than the major albumin of Pisum sativum . Extending the immunochemical study to members of the Phaseoleae, Glycineae, Cajaneae and Diocleae revealed that the vicilin and legumin of Cicer were more closely related to the Vicieae than to these tribes. Thus the data presented in this work recommended the classification of Cicer under Vicieae rather than as a separate tribe Cicerideae .

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