Hemoglobin lufkin: Β29 (b11) GLY→ASP an unstable hemoglobin variant involving an internal ahino acid residue

Robert M. Schmidt, Katherine C. Bechtel, Mary H. Johnson, Bradford L. Therrell, Winston F. Moo-Penn

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the β chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65°C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.

Original languageEnglish (US)
Pages (from-to)799-814
Number of pages16
JournalHemoglobin
Volume1
Issue number8
DOIs
StatePublished - 1977
Externally publishedYes

ASJC Scopus subject areas

  • Hematology
  • Clinical Biochemistry
  • Genetics(clinical)
  • Biochemistry, medical

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