Hb Rahere	beta82(EF6)Lys->Thr

CONTACT		2,3-DPG binding site
HEMATOLOGY		Mild polycythemia in the heterozygote
ELECTROPHORESIS		Hb X moves faster than Hb A at alkaline pH
CHROMATOGRAPHY		Hb X was isolated by DEAE-Sephadex chromatography
STRUCTURE STUDIES		Tryptic digestion; separation of peptides by reversed phase HPLC or fingerprinting; amino acid analysis
DNA ANALYSES		Not reported; presumed mutation AAG->ACG at codon 82
FUNCTION STUDIES		Increased oxygen affinity; normal Bohr effect and cooperativity; decreased 2,3-DPG binding
STABILITY		Normal
OCCURRENCE		Found in a Caucasian English male and a Japanese family
OTHER INFORMATION		Quantity in the heterozygote 48%

REFERENCES
1.		Lorkin, P.A., Stephens, A.D., Beard, M.E.J., Wrigley, P.F.M., Adams, L., and Lehmann, H.: Br. Med. J., 4:200, 1975.
2.		Sugihara, J., Imamura, T., Nagafuchi, S., Bonaventura, J., Bonaventura, C., and Cashon, R.: J. Clin. Invest., 76:1169, 1985.

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This material is from the book A Syllabus of Human Hemoglobin Variants (1996) by Titus H.J. Huisman, Marianne F.H. Carver, and Georgi D. Efremov, published by The Sickle Cell Anemia Foundation in Augusta, GA, USA. Copyright © 1996 by Titus H.J. Huisman. All rights reserved. Neither this work nor any part may be reproduced or transmitted in any form or by any means, electronic or mechanical, microfilming and recording, or by any information storage and retrieval systems, without written permission.