Linked Life Data

8343524

Source:http://linkedlifedata.com/resource/pubmed/id/8343524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-9-7
pubmed:abstractText
Reactivity of sulfhydryl groups of human uterine smooth muscle AMP-deaminase with DTNB, and the effect of their chemical modification on kinetic and regulatory properties of the enzyme were investigated. (1), Approx. 7 and 5 sulfhydryl groups per mol of the enzyme have been shown to be accessible for DTNB (5,5'-dithiobis(2-nitrobenzoic acid)) titration in denaturated and native AMP-deaminase, respectively. (2), Titrated groups were not homogenous; some of them reacted with DTNB much faster than others. (3), The activity of the modified enzyme was very low, and the modified enzyme manifested unusual hyperbolic saturation kinetics with the substrate. (4), Exhaustive dialysis against a buffer containing 10 mM thioethanol reactivated the modified enzyme, and restored its original regulatory properties. Experimental results obtained indicate that modified sulfhydryl groups play a significant role in the maintenance of the proper, catalytically-efficient conformation of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
1164
pubmed:geneSymbol
AMPD2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
261-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
AMP-deaminase from human uterine smooth muscle: the effect of DTNB treatment on kinetic and regulatory properties of the enzyme.
pubmed:affiliation
Department of Biochemistry, Academic Medical School, Gdansk, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't