Hb Nottingham beta98(FG5)Val->Gly
CONTACT Internal; heme and alpha1beta2 contacts
HEMATOLOGY Severe hemolytic anemia; reticulocytosis; Heinz bodies
ELECTROPHORESIS Hb X moves slightly faster then Hb A2 at alkaline pH
CHROMATOGRAPHY Hb X separates from Hb A by DEAE-cellulose chromatography; the betaX chain separates completely from the other chains by reversed phase HPLC (elution order: betaX, betaA, alpha)
STRUCTURE STUDIES Tryptic digestion of betaX chain; peptides were separated by reversed phase HPLC or fingerprinting; amino acid analysis; sequencing
DNA ANALYSES A GTG->GGG mutation at codon 98
FUNCTION STUDIES Increased oxygen affinity; decreased cooperativity
OCCURRENCE Found in a 2-year-old English female, in a 7-year-old Caucasian male from North Carolina, and in a 7-year-old Canadian male; all three are apparently de novo mutations
OTHER INFORMATION Quantity in the heterozygote ~26%
1. Gordon-Smith, E.C., Dacie, J.V., Blecher, T.E., French, E.A., Wiltshire, B.G., and Lehmann, H.: Proc. Roy. Soc. Med., 6:507, 1973.
2. Orringer, E.P., Felice, A.E., Reese, A., Wilson, J.B., Lam, H., Gravely, M.E., and Huisman, T.H.J.: Hemoglobin, 2:315, 1978.
3. Cepreganova, B., Wilson, J.B., Huisman, T.H.J., and Hume, H.A.: Hemoglobin, 16:77, 1992.

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.