Hb Rothschild	beta37(C3)Trp->Arg

CONTACT		alpha1beta2 contact
HEMATOLOGY		Nearly normal in the heterozygote; slight increase in reticulocytes
ELECTROPHORESIS		Hb X and Hb A separate at both alkaline and acidic pH; Hb X moves between Hb A2 and Hb S at high pH; it moves like Hb S at low pH; excellent separation by IEF
CHROMATOGRAPHY		Hb X separates from Hb A by anion exchange chromatography; elution order: A2-X-A
STRUCTURE STUDIES		Tryptic digestion; fingerprinting; amino acid analysis
DNA ANALYSES		Not reported; presumed mutation TGG->AGG or CGG at codon 37
FUNCTION STUDIES		Decreased oxygen affinity and cooperativity
STABILITY		Normal
OCCURRENCE		Found in a few Caucasian families
OTHER INFORMATION		Quantity in the heterozygote 37-50%; dissociates into dimers in the liganded state

REFERENCES
1.		Gacon, G., Belkhodja, O., Wajcman, H., and Labie, D.: FEBS Lett., 82:243, 1977.
2.		Craik, C.S., Vallette, I., Beychok, S., and Waks, M.: J. Biol. Chem., 255:6219, 1980.
3.		Danish, E.H., Harris, J.W., Ahmed, F., and Anderson, H.: Hemoglobin, 6:51, 1982.

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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.