Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-3-23
pubmed:abstractText
The slime mold Dictyostelium discoideum has two forms of the enzyme glycogen phosphorylase. The inactive phosphorylase 'b' form requires 5' AMP for activity and is present in early development. The active phosphorylase 'a' form is 5' AMP independent and occurs during later development. We here show that the 92 kd 'b' enzyme subunit exists either as a singlet or a doublet upon SDS-PAGE, depending on the method of sample extraction. In the presence of exogenously added Mn2+ and ATP, the phosphorylase 'b' shows apparent conversion into a 5' AMP independent form as measured by enzyme activity. In addition, Mn2+ and ATP also support an in vitro phosphorylation of the 92 kd phosphorylase 'b' subunit. We also demonstrate phosphorylation of the 'b' enzyme subunit in vivo by 32-P incorporation into the enzyme protein. A protein kinase responsible for the observed in vitro phosphorylation of the phosphorylase 'b' subunit is characterized.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
89-104
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Glycogen phosphorylase 'b' in Dictyostelium: stability and endogenous phosphorylation.
pubmed:affiliation
Biology Department, Virginia Tech, Blacksburg 24061.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.