Hemoglobin Ohio (beta 142 Ala replaced by): a new abnormal hemoglobin with high oxygen affinity and erythrocytosis.

Abstract:

:Hemoglobin Ohio [beta 142 (H20) Ala replaced by Asp] was found in three members of a white family, all of whom showed erythrocytosis. The variant hemoglobin has a high oxygen affinity, a reduced Bohr effect, and diminished cooperativity. The functional abnormalities of Hb Ohio are explained by the proximity of the substituent beta 142 residue, both to beta 143 His, which is involved in the DPG binding site of hemoglobin, and to the critical C terminal region of the beta chain, which participates in the stabilization of the deoxy (T) conformation.

journal_name

Blood

journal_title

Blood

authors

Moo-Penn WF,Schneider RG,Shih T,Jones RT,Govindarajan S,Govindarajan PG,Patchen LC

subject

Has Abstract

pub_date

1980-08-01 00:00:00

pages

246-50

issue

2

eissn

0006-4971

issn

1528-0020

journal_volume

56

pub_type

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