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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1980-1-19
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
570
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
248-58
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:387087-Amino Acids,
pubmed-meshheading:387087-Crystallization,
pubmed-meshheading:387087-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:387087-Escherichia coli,
pubmed-meshheading:387087-Macromolecular Substances,
pubmed-meshheading:387087-Molecular Weight,
pubmed-meshheading:387087-Pyruvate Kinase,
pubmed-meshheading:387087-Trypsin
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pubmed:year |
1979
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pubmed:articleTitle |
Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties.
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pubmed:publicationType |
Journal Article
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