| Literature DB >> 387087 |
G Valentini, P Iadarola, B L Somani, M Malcovati.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1979 PMID: 387087 DOI: 10.1016/0005-2744(79)90145-1
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002