Linked Life Data

6737095

Source:http://linkedlifedata.com/resource/pubmed/id/6737095

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-8-13
pubmed:abstractText
A thiamine-binding protein was purified from the extract of rice bran acetone powder by conventional procedures of acid precipitation, a series of column chromatography on DEAE-Sephadex A-50 and DEAE-cellulose, and gel filtration of Sephadex G-200. The purified thiamine-binding protein was nearly homogeneous as judged by disc gel electrophoresis and the molecular weight was estimated to be 94,000 by gel filtration on Sephadex Gn-200 and 50,000 by sodium dodecylsulfate (SDS) gel electrophoresis, suggesting that the protein is composed of two identical subunits. The apparent Kd and Bmax of the binding for [14C]thiamine was 0.44 +/- 0.05 microM and 17.2 +/- 0.7 nmol/mg of protein, respectively. The optimal pH for the binding is between 8.0 and 9.0. From the competition experiment using several thiamine derivatives, high binding specificity of the protein for thiamine was presumed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0301-4800
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-10
pubmed:dateRevised
2002-11-1
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Purification and some properties of thiamine-binding protein from rice bran.
pubmed:publicationType
Journal Article