Hb Cleveland	beta121(GH4)Glu->Gln;
	beta93(F9)Cys->Arg

HEMATOLOGY		Normal in the heterozygote
ELECTROPHORESIS		Hb X focuses between Hb S and Hb C
CHROMATOGRAPHY		Hb X elutes more slowly than Hb A2 from a cation exchange column; the betaX chain separates by reversed phase HPLC (elution order: betaX, betaA, delta, alpha)
STRUCTURE STUDIES		Tryptic digestion of betaX chain; separation of peptides by reversed phase HPLC; amino acid analysis; sequencing
DNA ANALYSES		Not reported; presumed mutations GAA->CAA and TGT->CGT at codons 121 and 93
FUNCTION STUDIES		Increased oxygen affinity; decreased Bohr effect and heme heme interaction
STABILITY		Decreased
OCCURRENCE		Found in an unidentified blood donor, a healthy 26-year-old female
OTHER INFORMATION		Quantity in the heterozygote ~40%; the beta93 Cys->Arg mutation is characteristic for Hb Okazaki and beta121 Glu->Gln for Hb D-Los Angeles

REFERENCES
1.		Wilson, J.B., Ramachandran, M., Webber, B.B., Kutlar, F., Hazelwood, L.F., Barnett, D., Hirschler, N.V., and Huisman, T.H.J.: Hemoglobin, 15:269, 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.