Hb Redondo beta92(F8)His->Asn->Asp
CONTACT Heme contact; proximal histidine
HEMATOLOGY Chronic hemolytic anemia in the heterozygote; reticulocytosis
ELECTROPHORESIS Hb X and Hb A separate at alkaline pH and by IEF; one band (X-Asn) was close to Hb A2, and the second (X-Asp) was between Hb A2 and Hb F
CHROMATOGRAPHY Two betaX chains separate from betaA by CM-cellulose chromatography and by reversed phase HPLC
STRUCTURE STUDIES Tryptic digestion of the AE-betaX chain; separation of the peptides by reversed phase HPLC; amino acid analysis; sequencing
DNA ANALYSES A CAC->AAC mutation at codon 92
FUNCTION STUDIES Oxygen dissociation curves were performed on stripped lysate (pH 7.2) and showed a slight decrease of the P50 value and a decrease of n50 in relation to the biphasic shape of the curve
OCCURRENCE Found as a de novo mutation in a Portuguese male and a Japanese female and her daughter
OTHER INFORMATION No metHb formation; Hb X readily loses its heme group; quantity of the two compounds in the heterozygote not reported
1. Wajcman, H., Vasseur, C., Blouquit, Y., Esperito Santo, D., Peres, M.J., Martins, M.C., Poyart, C., and Galacteros, F.: Am. J. Hematol., 38:194, 1991.
2. Harano, T., Harano, K., Kushida, Y., Ueda, S., Yoshii, A., and Nishinarita, M.: Hemoglobin, 15:279, 1991.

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.