Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-1-19
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
570
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-58
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties.
pubmed:publicationType
Journal Article