Open AccessThe Subunit Structure of Yeast Pyruvate Kinase
Author(s) -
BORNMANN Lothar,
HESS Benno
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03660.x
Subject(s) - cyanogen bromide , protein subunit , cleavage (geology) , biochemistry , pyruvate dehydrogenase complex , chemistry , yeast , valine , hydrolysis , amino acid , pyruvate kinase , stereochemistry , pyruvic acid , residue (chemistry) , acetylation , pyruvate dehydrogenase kinase , enzyme , peptide sequence , biology , paleontology , glycolysis , fracture (geology) , gene
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 an N ‐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.