Linked Life Data

6404625

Source:http://linkedlifedata.com/resource/pubmed/id/6404625

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-6-10
pubmed:abstractText
Sodium cholate at millimolar concentration is able to induce activity in rabbit muscle phosphorylase b in the absence of AMP. The maximum activation of the enzyme in presence of 7 mM sodium cholate was 24% of that achieved by 1 mM AMP. Other bile salts tested showed a negligible activating effect. The Ka for AMP was lowered fivefold by 5 mM of the steroid detergent, while the cooperative binding of the nucleotide was abolished. Phosphorylase b', a modified form of phosphorylase in which the phosphorylation site has been removed by limited tryptic attack, presented an activation profile similar to that of phosphorylase b. In contrast, phosphorylase a was inhibited by the bile salt, while the activity of liver phosphorylase b was not significantly affected. Modification of the AMP site of the enzyme with 2,3-butanedione could not inhibit sodium-cholate-induced activity. tert-Butanol, an organic solvent activator of phosphorylase b, was found to enhance the activity induced by sodium cholate. The interaction of sodium cholate and phosphorylase b was also followed by difference spectroscopy using a fluorescein isothiocyanate--phosphorylase b conjugate. Furthermore, measurements of electron spin resonance demonstrated that the mobility of a spin-label bound at buried--NH2 groups of phosphorylase b decreases cooperatively with increasing bile salt concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
625-31
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Effect of sodium cholate on the catalytic and structural properties of phosphorylase b.
pubmed:publicationType
Journal Article