Work

Hemoglobin Rahere, a human hemoglobin variant with amino acid substitution at the 2,3-diphosphoglycerate binding site. Functional consequences of the alteration and effects of bezafibrate on the oxygen bindings.

Year: 1985

Type: article

Abstract: We encountered an abnormal hemoglobin (Rahere), with a thre- onine residue replacing the ,682 (EF6) lysine residue at the bind- ing site of 2,3-diphosphoglycerate, which was responsible for overt erythrocytosis in two individuals of a Japanese family.Hemoglobin Rahere shows a lower oxygen affinity on the binding of 2,3-diphosphoglycerate or chloride ions than hemoglobin A. Although a decrease in the positive charge density at the binding sites of 2,3-diphosphoglycerate in hemoglobin Rahere apparently shifts the allosteric equilibrium toward the low affinity state, it greatly diminishes the cofactor effects by anions.The oxygen affinity of the patient's erythrocytes is substantially lowered by the presence of bezafibrate, which combines with sites different from those of 2,3-diphosphoglycerate in either hemoglobin Rahere or hemoglobin A.for the 1382 lysine residue at the binding site of 2,3-DPG (5).This study was undertaken to determine how this substitution affects the binding ofnatural anionic cofactors with hemoglobins,

Source: Journal of Clinical Investigation

DOI: 10.1172/jci112072

Authors: J Sugihara, T Imamura, S Nagafuchi, J Bonaventura, C Bonaventura, R Cashon

Institutions: Kyushu University, Duke University

Language: English

Topic: Hemoglobin structure and function

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze

Funder: Japan Society for the Promotion of Science