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
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.

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.