Linked Life Data

2268670

Source:http://linkedlifedata.com/resource/pubmed/id/2268670

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-2-21
pubmed:abstractText
The oxygen affinity of hemoglobin Sassari (Asp-126 alpha----His), a variant substituted in the alpha 1 beta 1 interface, was found to be 8-times greater relative to normal adult human hemoglobin. Study of the exchangeable hydrogen-bonded protons by NMR spectroscopy shows only minor changes at the alpha 1 beta 1 interface. In particular, the resonance previously assigned to the proton of the hydrogen bond Asp-126 alpha 1. . . Tyr-35 beta 1 in normal hemoglobin is still present in the variant spectrum, suggesting that His-126 alpha can also form a hydrogen bond with the Tyr-35 beta. The possible explanation of the increased affinity of hemoglobin Sassari and other variants substituted in the same structural region is discussed in terms of perturbations of the equilibrium between the two quaternary states.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
1041
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
250-3
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Functional and NMR studies of Hb Sassari (Asp-126 alpha----His); role of the inter-subunit contacts in the affinity control of human hemoglobin.
pubmed:affiliation
INSERM U.91 Hôpital Henri Mondor, Crêteil, France.
pubmed:publicationType
Journal Article, Comparative Study