Altered C-terminal salt bridges in haemoglobin York cause high oxygen affinity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1976-01

AUTHORS

GEORGE H. BARE, PHILIP A. BROMBERG, JAMES O. ALBEN, BERNADINE BRIMHALL, RICHARD T. JONES, SHELDON MINTZ, IRVING ROTHER

ABSTRACT

STUDIES of abnormal human haemoglobins (Hbs) with increased O2 affinity have been particularly useful in developing detailed molecular interpretations of normal Hb function. A number of functionally interesting mutants are altered in the βHC region but only one variant, Hb Hiroshima (β146 His→Asp)1,2, has been reported as having a substitution at the C terminus itself. We report here the structure and O2 equilibria of Hb York, a new mutation at the β146 position, His→Pro, associated with increased O2 affinity, decreased cooperativity and diminished Bohr effect. More... »

PAGES

155-156

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/259155a0

DOI

http://dx.doi.org/10.1038/259155a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036216989

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1246355


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