Linked Life Data

8155654

Source:http://linkedlifedata.com/resource/pubmed/id/8155654

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1994-5-13
pubmed:abstractText
The effects of chloride ion concentration on the rate constants for association of carbon monoxide with human hemoglobin A and a synthetic form of the mutant hemoglobin Rothschild (beta 37 Trp-->Arg) have been investigated by stopped-flow techniques. Previous studies of the structure [Kavanaugh et al. (1992) Biochemistry 31, 4111] and functional properties [Rivetti et al. (1993) Biochemistry 32, 2888] of hemoglobin Rothschild crystallized in the T state have demonstrated that the mutant arginine residues create new chloride ion binding sites and that chloride ions act to lower the oxygen affinity of hemoglobin Rothschild in these crystals. The studies reported here demonstrate a parallel effect of chloride ions on the rate of CO association with deoxygenated hemoglobin Rothschild in solution. Although the kinetics of CO binding to this hemoglobin in solution exhibit a Bohr effect, the chloride effect is independent of pH. In addition, we find that other halide ions have similar effects on the rate constants for the association of CO with this hemoglobin variant.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4363-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Chloride acts as a novel negative heterotropic effector of hemoglobin Rothschild (beta 37 Trp-->Arg) in solution.
pubmed:affiliation
School of Medicine and Biomedical Sciences, State University of New York at Buffalo.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.