Hb Helsinki	beta82(EF6)Lys->Met

CONTACT		2,3-DPG binding site
HEMATOLOGY		Erythrocytosis 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; CNBr splitting; fingerprinting; amino acid analysis
DNA ANALYSES		Not reported; presumed mutation AAG->ATG at codon 82
FUNCTION STUDIES		Increased oxygen affinity; decreased Bohr effect and 2,3-DPG binding; normal cooperativity
STABILITY		Not reported
OCCURRENCE		Found in members of four different Finnish families
OTHER INFORMATION		Quantity in the heterozygote not reported

REFERENCES
1.		Ikkala, E., Koskela, J., Pikkarainen, P., Rahiala, E-L., El-Hazmi, M.A.F., Nagai, K., Lang, A., and Lehmann, H.: Acta Haematol., 56:257, 1976.

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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.