Linked Life Data

3251563

Source:http://linkedlifedata.com/resource/pubmed/id/3251563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1989-8-9
pubmed:abstractText
The recent discovery of the negligible contribution of the triply ligated species to the oxygenation process of human hemoglobin A0 (S.J. Gill, E. Di Cera, M.L. Doyle, G.A. Bishop and C.H. Robert, Biochemistry 26 (1987) 3995) has pointed out the high precision of differential binding measurements. These measurements closely approximate the binding capacity (E. Di Cera, S.J. Gill and J. Wyman, Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 449) of the system and can be used to calculate higher derivatives of the binding curve. We develop here a new method for the determination of equilibrium constants through binding capacity measurements by which the physical parameters expressing the optical properties of the system are eliminated in the data analysis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-52
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
A new method for the determination of equilibrium constants through binding capacity measurements.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.