Linked Life Data

6456

Source:http://linkedlifedata.com/resource/pubmed/id/6456

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1976-8-23
pubmed:abstractText
Yeast alpha-isopropylmalate isomerase was found to be markedly stabilized by high concentrations of glycerol and (NH4)2SO4. Such conditions of high ionic strength inhibited the enzyme, stabilized the enzyme to heat, and affected kinetic parameters. The isomerase was found to exhibit ionic strength-dependent hysteresis when enzyme, totally but reversibly inhibited by storage under conditions of high ionic strength of (NH4)2SO4, was transferred to a lower concentration of (NH4)2SO4. Alpha-Isopropylmalate isomerase was found to be sensitive to KCN and certain other chelators. The inactivation by KCN was prevented by high concentrations of (NH4)2SO4. These observations implicated a metal involvement but the nature of the metal was not revealed. The metal involvement and some of the other properties of alpha-isopropylmalate isomerase reveal a similarity to aconitase. The similarities in properties between the isomerase and aconitase are summarized. Studies of yeast alpha-isopropylmalate isomerase indicated that it is a single polypeptide of about Mr = 90,000.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3545-52
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Yeast alpha-isopropylmalate isomerase. Factors affecting stability and enzyme activity.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.