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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1981-6-23
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pubmed:abstractText |
A new method for the purification of human erythrocyte uridylyl transferase (UDPglucose: alpha-D-galactose-1-phosphate uridylyltransferase EC 2.7.7.12) is described. It consists of a hydrophobic purification step associated with hydroxyapatite chromatography and provided for the first time a purification of more than 45 000-fold with a high activity (15 I.U/mg) and a yield of 32%. We show that the enzyme is a dimer and has a molecular weight of 88 000. It can be resolved into three bands by isoelectric focusing with an apparent pI between 5.0 and 5.4. It could be shown by steady-state initial rate measurements that the interconversion of the two substrates of human transferase (Gal-1-P and UDP-glucose) follows ping-pong bi-bi kinetics, with Km values of 0.2 and 0.065 mM, respectively.
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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 |
Feb
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
657
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
374-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6260202-Erythrocytes,
pubmed-meshheading:6260202-Humans,
pubmed-meshheading:6260202-Kinetics,
pubmed-meshheading:6260202-Macromolecular Substances,
pubmed-meshheading:6260202-Molecular Weight,
pubmed-meshheading:6260202-Nucleotidyltransferases,
pubmed-meshheading:6260202-Temperature,
pubmed-meshheading:6260202-UDPglucose-Hexose-1-Phosphate Uridylyltransferase
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pubmed:year |
1981
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pubmed:articleTitle |
Purification and characterization of human erythrocyte uridylyl transferase.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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