Linked Life Data

6715312

Source:http://linkedlifedata.com/resource/pubmed/id/6715312

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-6-7
pubmed:abstractText
Equilibrium and kinetic studies on the interaction between thermolysin (E) and its specific inhibitor (I), phosphoramidon (N-(alpha-L-rhamnopyranosyloxyphospho)-L-leucyl-L-tryptophan), have been made by steady-state inhibitory kinetics analysis, fluorometric titration and the stopped-flow method. The inhibitor constant, K1, the dissociation constant of the El complex, Kd, directly obtained by fluorometric titration, and the apparent second-order association constant, kon, obtained with the stopped-flow method are very similar to those for talopeptin (Kitagishi, K., et al. (1983) J. Biochem. 93, 47-53 and 55-59), whose molecular structure differs from that of phosphoramidon only in the configuration of the OH group at the C-4 atom of the sugar moiety. The result suggested that the OH group is not essential for the binding to thermolysin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
529-34
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Binding between thermolysin and its specific inhibitor, phosphoramidon.
pubmed:publicationType
Journal Article