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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1977-7-18
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pubmed:abstractText |
The AMP-activated pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) from Escherichia coli has been purified 200 times through a three-step procedure which gives a homogeneous preparation with a specific activity of 110. The enzyme appears to be a tetramer of molecular weight 190 000. Subunits (molecular weight 51 000) show a single amino-terminal amino acid (serine) and appear as a single band in polyacrylamide gel electrophoresis in sodium dodecyl sulphate. The enzyme crystallizes in conditions of reduced dielectric constant of the solvent in the pH range 6.5-7.5. Kinetic and regulatory properties of the purified enzyme are similar to those described for crude preparations of the enzyme.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
482
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
52-63
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:193572-Amino Acids,
pubmed-meshheading:193572-Crystallization,
pubmed-meshheading:193572-Cyclic AMP,
pubmed-meshheading:193572-Enzyme Activation,
pubmed-meshheading:193572-Escherichia coli,
pubmed-meshheading:193572-Fructosephosphates,
pubmed-meshheading:193572-Hexosediphosphates,
pubmed-meshheading:193572-Kinetics,
pubmed-meshheading:193572-Macromolecular Substances,
pubmed-meshheading:193572-Molecular Weight,
pubmed-meshheading:193572-Pyruvate Kinase
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pubmed:year |
1977
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pubmed:articleTitle |
Purification and molecular properties of the AMP-activated pyruvate kinase from Escherichia coli.
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pubmed:publicationType |
Journal Article
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