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Two forms of pyruvate kinase in Escherichia coli. a comparison of chemical and molecular properties

Valentini, G.; Iadarola, P.; Somani, B.L.; Malcovati, M.

Biochimica et Biophysica Acta 570(2): 248-258

1979


ISSN/ISBN: 0006-3002
PMID: 387087
DOI: 10.1016/0005-2744(79)90145-1
Accession: 041878649

The two forms of pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) present in Escherichia coli have been purified from the same cultures and crystallized. A modified procedure for the purification of type I pyruvate kinase is described. Molecular weight, subunit structure, amino acid composition, NH2-terminal amino acid, maps of tryptic peptides and conditions for crystallization have been determined for the two forms. A comparison of these data shows that the two forms are different proteins, each being a tetramer of identical subunits.

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