Linked Life Data

2751656

Source:http://linkedlifedata.com/resource/pubmed/id/2751656

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-8-14
pubmed:abstractText
Chymotrypsin-like activity of the multicatalytic proteinase (MCP) purified from eggs of the ascidian Halocynthia roretzi was activated by the addition of SDS. Complete activation was achieved simultaneously at the time of SDS addition, and this activity decreased as a function of time. Autonomous fluorescence of MCP also increased rapidly at the time of SDS addition and then decreased at a rate that depended on the SDS concentration. The decrease of autonomous fluorescence induced by SDS preceded that of the activity. These results suggest that a rapid conformational change of MCP induced by SDS results in the enhancement of chymotrypsin-like activity, followed by the decrease of this activity because of the lability of the activated conformation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
334-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Sodium dodecyl sulfate-induced conformational and enzymatic changes of multicatalytic proteinase.
pubmed:affiliation
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
pubmed:publicationType
Journal Article