Linked Life Data

7044001

Source:http://linkedlifedata.com/resource/pubmed/id/7044001

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10-11
pubmed:dateCreated
1982-7-8
pubmed:abstractText
The effects of disulfides (oxidized glutathione or cystine) and of cellular proteinases on rabbit muscle aldolase activity, thermal stability and susceptibility to proteolysis were determined. Native aldolase was reversibly inactivated by cystine and oxidized glutathione. Disulfide-inactivated aldolase had a lower transition temperature and enthalpy for denaturation than the native enzyme and was extensively degraded by lysosomal enzymes or a metallo-proteinase, meprin. Native aldolase was also inactivated by lysosomal enzymes or meprin; this inactivation was due to limited proteolysis in the C-terminus. However, aldolase inactivated by limited proteolysis had the same thermal stability as native aldolase and was resistant to extensive proteolysis by lysosomal enzymes or meprin. These data provide insight into the molecular basis whereby formation of mixed disulfides between proteins and glutathione or cysteine may result in unstable protein conformations and may be an initial event in the process of degradation of soluble cellular enzymes to amino acids and small peptides.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5318
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1365-74
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Initial events in the degradation of soluble cellular enzymes: factors affecting the stability and proteolytic susceptibility of fructose-1,6-bisphosphate aldolase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't