Two forms of pyruvate kinase in Escherichia coli a comparison of chemical and molecular properties
Copyright policy )Two forms of pyruvate kinase in Escherichia coli a comparison of chemical and molecular properties
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.
- University of Pavia Italy
570, isoenzymes, Macromolecular Substances, Pyruvate Kinase, E. coli, Molecular Weight, Escherichia coli, Electrophoresis, Polyacrylamide Gel, Trypsin, Amino Acids, Crystallization, Pyruvate kinase
570, isoenzymes, Macromolecular Substances, Pyruvate Kinase, E. coli, Molecular Weight, Escherichia coli, Electrophoresis, Polyacrylamide Gel, Trypsin, Amino Acids, Crystallization, Pyruvate kinase
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).34 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!