Hb S-Providence beta6(A3)Glu->Val;
HEMATOLOGY Normal in the heterozygote
ELECTROPHORESIS Hb X and Hb A do not separate by routine electrophoresis at either alkaline or acidic pH
CHROMATOGRAPHY Not reported; the betaX and betaA chains separate by CM-cellulose chromatog-raphy
STRUCTURE STUDIES tryptic digestion of AE-betaX chain; separation of peptides by fingerprinting; amino acid analysis; sequencing
DNA ANALYSES Not reported; presumed mutations GAG->GTG and AAG->AAT or AAC at codons 6 and 82
FUNCTION STUDIES Sickling test is positive; increased oxygen affinity
OCCURRENCE Found in a West African female
OTHER INFORMATION The beta82 position is part of the 2,3-DPG binding site; the beta82 Lys->Asn replacement is characteristic for Hb Providence; both Hb Providence and Hb S-Providence have a tendency to become deamidated
1. Gale, R.E., Blair, N.E., Huehns, E.R., and Clegg, J.B.: Br. J. Haematol., 70:251, 1988.

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.