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A novel sickle hemoglobin: hemoglobin S-south end.

Authors
  • Luo, Hong-Yuan
  • Adewoye, Adeboye H
  • Eung, Shawn H
  • Skelton, Timothy P
  • Quillen, Karen
  • McMahon, Lillian
  • Steinberg, Martin H
  • Chui, David H K
Type
Published Article
Journal
Journal of Pediatric Hematology/Oncology
Publisher
Ovid Technologies (Wolters Kluwer) - Lippincott Williams & Wilkins
Publication Date
Nov 01, 2004
Volume
26
Issue
11
Pages
773–776
Identifiers
PMID: 15543018
Source
Medline
License
Unknown

Abstract

Sickle hemoglobin (Hb S; beta Glu6Val) is due to an A<T transversion in codon 6 of the beta-globin gene. Several Hb S variants have both the Hb S mutation plus another mutation in the same beta-globin gene. Some of these variant hemoglobins can lead to sickle cell disease even in the simple heterozygote. Moreover, some variant hemoglobins mimic Hb A, S, or C on one or several clinical laboratory diagnostic tools, thus making their correct identification potentially problematic. The authors report a novel Hb S variant hemoglobin, Hb S-South End (beta Glu6Val, GAG>GTG; 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.

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