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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1977-9-22
|
| pubmed:abstractText |
Rabbit muscle phosphorylase b was found to be capable of forming protein bound alpha-1,4 glucosyl chains upon incubation of the enzyme with appropriate concentrations of glucose-1-phosphate with no primer addition (unprimed synthesis). This activity would only be present in a small fraction of the total muscle phosphorylase b activity, as judged from the high concentrations of enzyme which are required to demonstrate the occurrence of unprimed synthesis. Polyacrylamide gel electrophoresis shows the presence of a phosphorylase isoenzyme capable of accepting glucosyl moieties, giving rise to a glucosylated protein enzymatically active in the chain lengthening of its own glucan.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0300-8177
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
16
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
141-8
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:18666-Animals,
pubmed-meshheading:18666-Glycogen,
pubmed-meshheading:18666-Hydrogen-Ion Concentration,
pubmed-meshheading:18666-Kinetics,
pubmed-meshheading:18666-Muscles,
pubmed-meshheading:18666-Phosphorylases,
pubmed-meshheading:18666-Rabbits,
pubmed-meshheading:18666-Structure-Activity Relationship
|
| pubmed:year |
1977
|
| pubmed:articleTitle |
A primer independent activity of rabbit muscle phosphorylase b.
|
| pubmed:publicationType |
Journal Article
|