Isolation and characterization of a minor legumin and its constituent polypeptides from Pisum sativum (pea)

March, J. F., Pappin, D. J., Casey, R. (March 1988) Isolation and characterization of a minor legumin and its constituent polypeptides from Pisum sativum (pea). Biochem J, 250 (3). pp. 911-5. ISSN 0264-6021 (Print)0264-6021 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/3390145

Abstract

The purification and characterization of a minor legumin species from Pisum sativum is described. Electrophoretic data indicate that it corresponds to a legumin subunit pair previously designated L1. The beta-polypeptides of the minor legumin have a phenylalanine N-terminus. This is the first time that an amino acid other than glycine has been reported as the N-terminus of the basic polypeptides from legumin-like proteins from any plant species. Sequence analyses of the isolated alpha- and beta-polypeptides of the minor legumin show that it does not correspond to any of the three legumin gene families that have previously been defined on the basis of DNA hybridizations and genetic analyses.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Fabaceae/ analysis Molecular Sequence Data Peptide Fragments/ analysis Plant Proteins Plants, Medicinal Vegetable Proteins/ isolation & purification
Subjects: organism description > plant
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > polypeptides
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Matt Covey
Date: 15 March 1988
Date Deposited: 18 Sep 2014 16:28
Last Modified: 18 Sep 2014 16:28
PMCID: PMC1148942
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30762

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