Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-2-21
pubmed:abstractText
The self-association of diisopropylphosphoryl(DIP)-alpha-chymotrypsin is studied in order to find out whether the active site of the enzyme is involved in its self-association behaviour or not. Sedimentation coefficient as well as the weight-average (Archibald) molecular weight data are obtained as a function of concentration using an analytical ultracentrifugation technique. The analysis indicated that the experimental data fits the model of indefinite self-association. The comparison of the data with earlier data on alpha-chymotrypsin revealed that after the modification at the active site, the association constant for the self-association is reduced by about 47%, and the system deviated from ideality. Results showed further that Ser-195, at the active site, appears to be involved in the self-association behaviour of alpha-chymotrypsin; however, the participation of other groups at the active site is also implicated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
1041
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-90
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Self-association of diisopropylphosphoryl-alpha-chymotrypsin: the involvement of active site of the enzyme in its self-association behaviour.
pubmed:affiliation
Centre for Cellular and Molecular Biology, Hyderabad, India.
pubmed:publicationType
Journal Article