Hb J-Rovigo alpha53(E2)Ala->Asp
CONTACT External
HEMATOLOGY Normal in the heterozygote
ELECTROPHORESIS Hb X moves faster than Hb A at alkaline pH; Hb X does not separate from Hb A at acidic pH
STRUCTURE STUDIES Tryptic digestion; separation of peptides by fingerprinting; amino acid analysis
DNA ANALYSES Not reported; presumed mutation GCC->GAC; alpha2 or alpha1
FUNCTIONAL STUDIES Normal oxygen affinity, Bohr effect, and cooperativity
STABILITY Probably normal
OCCURRENCE Found in Italian and Brazilian families
OTHER INFORMATION Quantity in heterozygotes 20-30%; found in combination with beta-thal
1. Alberti, R., Mariuzzi, G.M., Artibani, L., Bruni, E., and Tentori, L.: Biochim. Biophys. Acta, 342:1-1974.
2. Moo-Penn, W.F., Jue, D.L., and Baine, R.M.: Hemoglobin, 2:443, 1978.
3. Targino de Araujo, J., Plowman, D., Targino de Araujo, R.A., de Souza, L.F., and Lehmann, H.: Rev. Bras. Pesq. Med. Biol., 13:37, 1980.

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.