Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-2-18
pubmed:abstractText
The rat testicular galactolipid sulfotransferase has been purified by affinity chromatography using 3'5'-adenosine diphosphate-agarose affinity chromatography. Both galactosyl glycerolipid and galactosyl ceramide were effective substrates with Km values of 4.8 and 1.1 microM respectively. A single protein of molecular mass 56 kDa was present in the purified sulfotransferase preparation as monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining. Specific photoaffinity substrate labeling, using an azido derivative of galactosyl ceramide, was used to identify this protein, both in crude extracts and when purified. The protein was also selectively phosphorylated in the presence of the rat testicular galactolipid sulfotransferase stimulatory protein kinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1655-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Purification of the testicular galactolipid: 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase.
pubmed:affiliation
Research Institute, Hospital for Sick Children, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't