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Hemoglobin Okayama [β‐2 (NA 2) His → Gln]: A new ‘silent’ hemoglobin variant with substituted amino acid residue at the 2,3‐diphosphoglycerate binding site
Author(s) -
Harano Teruo,
Harano Keiko,
Shibata Susumu,
Ueda Satoshi,
Mori Hiroo,
Arimasa Naomichi
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80239-7
Subject(s) - diphosphoglycerate , hemoglobin , chemistry , amino acid residue , residue (chemistry) , biochemistry , binding site , stereochemistry , peptide sequence , gene
A new ‘silent’ abnormal hemoglobin, Hb Okayama [β2 (NA 2) His → Gln], happened to be discovered in a diabetic Japanese female living in Okayama Prefecture, Japan, in the course of glyco‐Hb measurement of the blood samples of diabetic patients. This variant did not differ from Hb A by conventional electrophoretic tests. Only the isoelectric focusing on PAG plate for the determination of glyco‐Hb and the cation exchanger chromatography were successful in the separation of this abnormal variant from Hb A and glyco‐Hb. Functional study of the whole blood demonstrated a slight increase of oxygen affinity.