MUTATION		Codon 124 (-A); CCA(Pro)->CC-
AMINO ACID REPLACEMENT		Extended beta chain
TYPE OF BETA-THAL		Dominant, inclusion body beta-thal trait
MECHANISM		The deletion of A creates a frameshift with a terminating codon at codon 157 (TAA); the extended betaX chain (156 amino acids) is unstable and catabolized causing this TYPE OF BETA-THAL
IDENTIFICATION		Amplification of the beta-globin gene; DNA sequencing; dot-blot analysis with allele specific probes
HEMATOLOGY IN HETEROZYGOTE(S)		Hb 5-8 g/dl; reticulocytes 1.0-3.5%; Heinz bodies
HEMATOLOGY IN HOMOZYGOTE(S)		None
OCCURRENCE		Found in an 18-year-old Russian male
HAPLOTYPE		Not determined
FOUND IN COMBINATION WITH ABNORMAL HB(S)		Not reported
FOUND IN COMBINATION WITH BETA-THAL ALLELE(S)		Not reported
OTHER INFORMATION		The betaX chain could not be detected

REFERENCES
1.		Çürük, M.A., Molchanova, T.P., Postnikov, Yu.V., Pobedimskaya, D.D., Liang, R., Baysal, E., Kolodey, S., Smetanina, N.S., Tokarev, Yu.N., Rumyantsev, A.G., and Huisman, T.H.J.: Am. J. Hematol., 46: 329, 1994.

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This material is from the book A Syllabus of Thalassemia Mutations (1997) by Titus H.J. Huisman, Marianne F.H. Carver, and Erol Baysal, published by The Sickle Cell Anemia Foundation in Augusta, GA, USA. Copyright © 1997 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 permission in writing from the Author.