Hb Deer Lodge beta2(NA2)His->Arg
CONTACT 2,3-DPG binding site
HEMATOLOGY Normal in the heterozygote
ELECTROPHORESIS Hb X moves between Hb A and Hb S at alkaline pH
CHROMATOGRAPHY Separation of Hb A, Hb S, and Hb X by cation exchange HPLC
STRUCTURE STUDIES Tryptic digestion; fingerprinting; amino acid analysis; cation exchange chromatography; HPLC
DNA ANALYSES Not reported; presumed mutation CAC->CGC at codon 2
FUNCTION STUDIES Increased oxygen affinity, particularly below pH 6 and above pH 8; decreased cooperativity and slight increase in Bohr effect; cooperativity restored and Bohr effect reduced with the addition of 2,3-DPG and IHP
OCCURRENCE Found in a few Welsh-Dutch-English and Black families; one was also heterozygous for Hb S
OTHER INFORMATION Quantity in the heterozygote 40-45%
1. Labossiere, A., Vella, F., Hiebert, J., and Galbraith, P.: Clin. Biochem., 5:46, 1972.
2. Bonaventura, J., Bonaventura, C., Sullivan, B., and Godette, G.: J. Biol. Chem., 250: 9250, 1975.
3. Powars, D., Schroeder, W.A., Shelton, J.R., Evans, L., and Vinetz, R.: Hemoglobin, 1: 97, 1977.

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.