Yeast pyruvate kinase (Saccharomyces carlsbergensis) contains four identical subunits based on the following observations.1. Cyanogen bromide cleavage yields eight peptides as expected for identical subunits from the amino acid composition.2. No free N‐terminal residue could be detected. Upon acid hydrolysis 1 mole of acetate is liberated per mole of subunit. Differential hydrazinolysis indicates that anN‐acetylated terminus of the subunit is the source of the acetate molecule.3. Cleavage with carboxypeptidase A in the presence of sodium dodecylsulphate revealed that valine is the C‐terminal amino acid.
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