2 forms of pyruvate kinase ec 184.108.40.206 in escherichia coli a comparison of chemical and molecular properties
Valentini, G.; Iadarola, P.; Somani, B.L.; Malcovati, M.
Biochimica et Biophysica Acta 70(2): 248-258
The 2 forms of pyruvate kinase (ATP: pyruvate 2-O-phosphotransferase, EC 220.127.116.11) present in E. coli were purified from the same cultures and crystallized. A modified procedure for the purification of type I pyruvate kinase is described. MW, subunit structure, amino acid composition, NH2-terminal amino acid, maps of tryptic peptides and conditions for crystallization were determined for the 2 forms. A comparison of these data shows that the 2 forms are different proteins, each being a tetramer of identical subunits.