Linked Life Data

6766324

Source:http://linkedlifedata.com/resource/pubmed/id/6766324

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-4-26
pubmed:abstractText
1. The refolding of rabbit muscle creatine kinase (ATP:creatine N-phosphotransferase, EC 2.7.3.2) which had been denatured in 3 M guanidine hydrochloride was monitored by studying the regain of enzyme activity. Full activity could be regained provided that the residual denaturant concentration was less than or equal to 0.1 M. 2. The refolded product was shown by a number of criteria (CD, kinetic parameters and polyacrylamide gel electrophoresis) to be identical with the native enzyme. 3. The rate of regain of enzyme activity was studied as a function of protein concentration. It was found that 70% of the activity was regained in a rapid, first-order process. The remaining activity was regained more slowly. In the rapid phase the number of reactive thiol groups per subunit declined from four to two; the further decline to one per subunit occurred more slowly. 4. It was found that the presence of the reducing agent dithiothreitol was not necessary for the regain of full activity, provided that the chelating agent EDTA was present. 5. The subunit structure of the enzyme during refolding was studied using dimethylsuberimidate as a cross-linking agent. From these experiments, a pathway for the refolding process could be proposed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
621
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-14
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
The refolding of denatured rabbit muscle creatine kinase.
pubmed:publicationType
Journal Article