Hb Cranston	beta144+beta145 (+AA); abnormal C-terminal sequence:
	(144)Lys-(145)SER-Ile-Thr-Lys-Leu-Ala-Phe-
	Leu-Leu-Ser-Asn-Phe-(157)Tyr-COOH

HEMATOLOGY		Compensated hemolytic anemia in the heterozygote
ELECTROPHORESIS		Hb X moves close to Hb S at alkaline pH
CHROMATOGRAPHY		Hb X was isolated on a DEAE-cellulose column
STRUCTURE STUDIES		Tryptic digestion of AE-betaX chain; separation of peptides by fingerprinting; amino acid analysis; sequencing
DNA ANALYSES		Not reported; presumed frameshift at codon beta145 (+AG)
FUNCTION STUDIES		Increased oxygen affinity; decreased Bohr effect and coop-erativity
STABILITY		Unstable; dissociation of subunits, hybrids
OCCURRENCE		Found in members of an Italian-American family
OTHER INFORMATION		Quantity in the heterozygote 30-40%

REFERENCES
1.		Bunn, H.F., Schmidt, G.J., Haney, D.N., and Dluhy, R.G.: Proc. Natl. Acad. Sci. USA, 72:3609, 1975.
2.		McDonald, M.J., Lund, D.P., Bleichman, M., Bunn, H.F., DeYoung, A., Noble, R.W., Foster, B., and Arnone, A.: J. Mol. Biol., 140:357, 1980.
3.		Shaeffer, J.R., Schmidt, G.J., Kingston, R.E., and Bunn, H.F.: J. Mol. Biol., 140: 377, 1980.

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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.