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Electrophoretic Studies on Seed Protein of the Genus Lathyrus

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Abstract

SDS-polyacrylamide gel electrophoresis of total seed extracts revealed the presence of legumin-like polypeptides ranging in molecular weight from 42 kD to 89 kD in Lathyrus sativus and L. odoratus. The polypeptides of higher mol wt were however, absent in L. aphaca. Vicilin-like polypepides of mol wt 76, 54, 36, 33, 31, 20 and 17 kD were seen in L. sativus and L. odoratus and of mol wt 72, 58, 54, 52, 36, 33 and 20 kD in L. aphaca. Analysis of various seed protein fractions of L. sativus revealed the presence of a large number of albumin polypeptides varyingin mol wt range from 12.5 to 95 kD, when as glutelin (mol wt 18 to 80 kD) and prolamin (mol wt 25.5 and 26 kD) fraction polypeptides were relatively fewer. On the basis of similarities in seed polypeptide profiles, L. sativus and L. odoratus seem to be closely related, whereas L. aphaca appears to be distantly related.

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Authors and Affiliations

  1. Department of Botany, Kurukshetra University, Kurukshetra, 132 119, India

    Anita Sood, Mamta Chandna & N. K. Matta

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  1. Anita Sood
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  2. Mamta Chandna
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  3. N. K. Matta
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Sood, A., Chandna, M. & Matta, N.K. Electrophoretic Studies on Seed Protein of the Genus Lathyrus . J. Plant Biochem. Biotechnol. 4, 121–124 (1995). https://doi.org/10.1007/BF03262967

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  • DOI: https://doi.org/10.1007/BF03262967

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