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.