Linked Life Data

7417456

Source:http://linkedlifedata.com/resource/pubmed/id/7417456

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-12-18
pubmed:abstractText
Trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.2) covalently immobilized on Sepharose or in polyacrylamide gel has been irreversibly denatured at 70--90 degrees C and then reactivated in an almost 100% yield. Thermoinactivated enzyme is first made to unfold under the action of urea with S-S bonds being simultaneously reduced and then made to refold (under the optimal conditions for the thiol-disulfide exchange) into its native conformation. It is demonstrated that the 'irreversible monomolecular thermoinactivation-reactivation' cycle can be repeated many times. The contribution of various mechanisms to thermoinactivation of the enzymes is discussed. Based on the data obtained, the irreversible thermoinactivation of enzymes under investigation should be ascribed only to changes in their secondary and teritary structures; the primary structure is not likely to be affected.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
615
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
426-35
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Reactivation of enzymes irreversibly denatured at elevated temperature. Trypsin and alpha-chymotrypsin covalently immobilized on Sepharose 4B and in polyacrylamide gel.
pubmed:publicationType
Journal Article