Linked Life Data

9784846

Source:http://linkedlifedata.com/resource/pubmed/id/9784846

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-12-11
pubmed:abstractText
Properties of soluble thiamine triphosphatase (ThTPase), adenosine triphosphatase, nucleoside triphosphatase and alkaline phosphatase activities in bovine kidney were compared. ThTPase and the other phosphatases differed clearly in their pH-dependences, K(m) and molecular masses. Apparent K(m) and pH optimum for ThTPase were determined to be 45.5 microM and 8.9, respectively. Molecular mass of the enzyme was 29.1 kDa as estimated by Sephadex G-100 gel filtration. The results obtained show bovine kidney to contain a specific soluble ThTPase, this enzyme being the only one hydrolyzing low concentrations of ThTP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Thiamine triphosphatase activity in bovine kidney.
pubmed:affiliation
Laboratory of Applied Enzymology and Biotechnology, Academy of Sciences of Belarus, Grodno. averin@biochem.belpak.grodno.by
pubmed:publicationType
Journal Article