Hb Himeji	beta140(H18)Ala->Asp

CONTACT		Internal
HEMATOLOGY		Normal in the heterozygote
ELECTROPHORESIS		Hb X and Hb A can be separated by routine methodology; Hb X moves faster than Hb A; excellent separation by IEF
CHROMATOGRAPHY		Hb X and Hb A separate in cation exchange HPLC; the betaX and betaA chains separate by reversed phase HPLC (elution order: betaX, betaA, alpha)
STRUCTURE STUDIES		Tryptic digestion of betaX chain; separation of peptides by reversed phase HPLC; amino acid analysis; sequencing
DNA ANALYSES		Not reported; presumed mutation GCC->GAC at codon 140
FUNCTION STUDIES		Increased oxygen affinity; normal Bohr effect
STABILITY		Slightly unstable
OCCURRENCE		Found in a 52-year-old Japanese male, and in two members of a Portuguese family
OTHER INFORMATION		Quantity in the heterozygote ~21%; increased binding of glucose at the amino terminus of the beta chain

REFERENCES
1.		Ohba, Y., Miyaji, T., Murakami, M., Kadowaki, S., Fujita, T., Oimomi, M., Hata-naka, H., Ishikawa, K., Baba, S., Hitaka, K., and Imai, K.: Hemoglobin, 10:109, 1986.
2.		Martins, M.C., Rosado, L., Wilson, J.B., Kutlar, A., Hu, H., and Huisman, T.H.J.; Hemoglobin, 13:411, 1989.
3.		Lavinha, J., Faustino, P., Osório-Almeida, L., Hattori, Y., Ohba, Y., and Martins, M.C.: Hemoglobin, 15:137, 1991.

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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.