Comparison of the subunit and primary structures of the pyruvate kinases from rabbit and sturgeon muscles

Author:

Anderson P J1,Randall R F1

Affiliation:

1. Department of Biochemistry, University of Ottawa, Ont. K1N 6N5, Canada

Abstract

The structures of the pyruvate kinases isolated from rabbit and sturgeon muscles were compared. Both enzymes are composed of subunits of 56000 mol.wt. Amino acid compositions of the two enzymes are similar, but not identical. Examination of the peptides produced by CNBr cleavage demonstrated that there are at least some highly homologous regions in the two proteins. There are only two replacements between an 18-residue portion of the polypeptide chain of rabbit muscle pyruvate kinase and a portion of the polypeptide chain of the enzyme isolated from sturgeon muscle.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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