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
STABILITY		Unstable
OCCURRENCE		Found in two unrelated Caucasian adults but not in their parents
OTHER INFORMATION		Quantity in the heterozygote 36%

REFERENCES
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.

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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.