Linked Life Data

6088322

Source:http://linkedlifedata.com/resource/pubmed/id/6088322

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1984-10-19
pubmed:abstractText
Galactosyltransferase from bovine milk was inactivated by a series of sulfhydryl group specific reagents of different structures and sizes. The inactivation rate constants suggest that the thiol is located in a nonpolar microenvironment. The ESR spectrum of a spin labeled galactosyltransferase showed that the sulfhydryl group is in a region of non-restricted rotation, consistent with its broad reactivity towards various thiol reagents. Galactosyltransferase immobilized onto agarose through its sulfhydryl group retained its ability to catalyze the synthesis of N-acetyllactosamine and lactose. Thus the residual activity of the sulfhydryl group modified enzyme is not due to an isozyme lacking such a group. In addition, the active thiol can not be located at the active site nor the protein-protein interaction site between galactosyltransferase and alpha-lactalbumin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-711X
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
913-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The sulfhydryl group microenvironment of lactose synthase from bovine milk.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.