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
OCCURRENCE Found in a few Caucasian families
OTHER INFORMATION Quantity in the heterozygote 37-50%; dissociates into dimers in the liganded state
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.

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.