Linked Life Data

1699799

Source:http://linkedlifedata.com/resource/pubmed/id/1699799

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1990-12-4
pubmed:abstractText
Crystalline preparations of glycogen phosphorylase b contain traces of acid phosphatase activity. Non-denaturing gel electrophoresis of phosphorylase b reveals a single band of 1-naphthyl phosphate phosphohydrolase activity which co-migrates with phosphorylase. The two enzymes can be separated by Sephadex G-200 column chromatography, where the phosphatase exhibits an apparent Mr of 17,000. The contaminant enzyme hydrolyzes effectively the phenolic ester of monoorthophosphate with optimal activity for p-nitrophenyl phosphate and L-phosphotyrosine between pH 5.5 and 6.0. The phosphatase is insensitive to inhibition by L(+)-tartrate but strongly inhibited by microM vanadate and Zn2+.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
76-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
A low-molecular weight acid phosphatase present in crystalline preparations of rabbit skeletal muscle glycogen phosphorylase b.
pubmed:affiliation
Institute of Biological Research, National Hellenic Research Foundation, Athens, Greece.
pubmed:publicationType
Journal Article