Linked Life Data

791944

Source:http://linkedlifedata.com/resource/pubmed/id/791944

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1977-1-29
pubmed:abstractText
The dye tetraiodofluorescein (TIF) was found to be an effective inhibitor of yeast hexokinase. It is a competitive inhibitor relative to MgATP2- and a noncompetitive inhibitor of glucose binding, a kinetic pattern consistent with the previously proposed random kinetic mechanism. TIF interacts directly with the native dimeric protein to give a difference spectrum with a maximum at 543 nm. Monomeric protein (produced by addition of 0.6 M NaCl) interacts with TIF to give a slightly altered difference spectrum, with the gammamax at 545 nm. The difference spectrum of the dimeric form is not perturbed by the addition of substrates but the absorbance with the monomer is lowered by MgATP2-. The Kd for MgATP2- was estimated to be 7 nM for monomeric hexokinase. These results suggest that results of previous binding studies with hexokinase at high concentrations which have been interpreted as being at variance with kinetic studies are due likely to different conformations of the protein under different experimental conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7157-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Interaction of tetraiodofluorescein with yeast hexokinase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.