Hb Wayne	alpha139 (-A) in alpha2 or alpha1; modified C-terminal sequence:
	(139)ASN-Thr-Val-Lys-Leu-Glu-Pro-(146)Arg-COOH

HEMATOLOGY		Normal in the heterozygote
ELECTROPHORESIS		Hb X appears as two bands (one band cathodic and the other anodic to Hb J-Baltimore) in electrophoresis at alkaline pH
CHROMATOGRAPHY		Hb X elutes faster than Hb A from a cation exchange HPLC column; can also be isolated on DEAE-Sephadex or DEAE-Sephacel columns
STRUCTURE STUDIES		Tryptic digestion of alphaX chain; separation of peptides by fingerprinting or reversed phase HPLC; amino acid analysis; sequencing; Edman degradation
DNA ANALYSES		Not reported; variation must be the result of a frameshift
FUNCTION STUDIES		Increased oxygen affinity; decreased cooperativity and Bohr effect
STABILITY		Stable
OCCURRENCE		Found in members of three Caucasian families in the USA
OTHER INFORMATION		Quantity in the heterozygote 12-16%

REFERENCES
1.		Seid-Akhavan, M., Winter, W.P., Abramson, R.K., and Rucknagel, D.L.: Proc. Natl. Acad. Sci. USA, 73:82, 1976.
2.		Huisman, T.H.J., Headlee, M.G., Wilson, J.B., Lam, H., Johnson, S.E.N., and Webber, B.B.: Hemoglobin, 8:1, 1984.

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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.