Hb Djelfa beta98(FG5)Val->Ala
CONTACT Internal; heme and alpha1beta2 contacts
HEMATOLOGY Normal but with a modest reticulocytosis and Heinz body formation
ELECTROPHORESIS Hb X moves anodal to Hb A2 at alkaline pH and by IEF
CHROMATOGRAPHY The betaX chain separates completely from the other chains by reversed phase HPLC (elution order: betaX, betaA, alpha)
STRUCTURE STUDIES Tryptic digestion of betaX chain; separation of peptides by reversed phase HPLC or by fingerprinting; amino acid analysis
DNA ANALYSES Not reported; presumed mutation GTG->GCG at codon 98
FUNCTION STUDIES Increased oxygen affinity; decreased cooperativity; normal Bohr effect
OCCURRENCE Found in two unrelated Caucasian adults but not in their parents
OTHER INFORMATION Quantity in the heterozygote 36%
1. Gacon, G., Wajcman, H., Labie, D., and Cosson, A.: FEBS Lett., 58:238, 1975.
2. Gacon, G., Krishnamoorthy, R., Wajcman, H., Labie, D., Tapon, J., and Cosson, A.: Biochim. Biophys. Acta, 490:156, 1977.
3. Bird, A.R., Elliott, T., Wilson, J.B., Webber, B.B., Hu, H., Kutlar, A., Kutlar, F., and Huisman, T.H.J.: Hemoglobin, 13:193, 1989.

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.