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2 forms of pyruvate kinase ec 2.7.1.40 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

1979

ISSN/ISBN: 0005-2728
Accession: 004535706
The 2 forms of pyruvate kinase (ATP: pyruvate 2-O-phosphotransferase, EC 2.7.1.40) 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.

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Related References

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