A Novel Sickle Hemoglobin: Hemoglobin S-South End

Abstract

Sickle hemoglobin (Hb S; beta Glu6Val) is due to an AGTG; beta Lys132Asn, AAA>AAC). When present alone, the beta Lys132Asn mutation has low oxygen affinity. Therefore, this mutation may enhance the polymerization of the Hb S variant. Furthermore, the variant hemoglobin mimics Hb A on high-pressure liquid chromatography, and its identity is not easily diagnosed. A succinct review of variant sickle hemoglobins is also presented.

Authors

Luo H-Y; Adewoye AH; Eung SH; Skelton TP; Quillen K; McMahon L; Steinberg MH; Chui DHK

Journal

Journal of Pediatric Hematology/Oncology, Vol. 26, No. 11, pp. 773–776

Publisher

Wolters Kluwer

Publication Date

November 1, 2004

DOI

10.1097/00043426-200411000-00019

ISSN

1077-4114

Associated Experts

David Hing-kwei Chui

Professor Emeritus, Faculty of Health Sciences

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