Hemoglobin Fannin-Lubbock [α2β2119(GH2) Gly → Asp]. A New Hemoglobin Variant at the α1β1 Contact

Winston F. Moo-Penn, Katherine C.Bechtel, Mary H. Johnson, Danny L. Jue, L. Bradford, Jr Therrell, Barbara Y. Morrison, Robert M. Schmidt

Research output: Contribution to journalArticlepeer-review


Hemoglobin Fannin-Lubbock was found in a 9-year-old Mexican-American female. The abnormal hemoglobin was detected as a fast-moving variant by electrophoresis on cellulose acetate at pH 8.4. Structural analysis indicated a substitution in the β-chain of aspartic acid for glycine at position 119, a position involved in the α1β1 contact of the hemoglobin tetramer. This contact between unlike chains is larger and undergoes a smaller shift during the process of oxygenation and deoxygenation than the α1β2 contact (Perutz, M.F., Muirhead, H., Cox, J.M. and Goaman L.C.G. (1968) Nature 219, 131-139). Mutations in this contact tend to cause slight or no changes in functional behavior. Apart from a mild anemia, the propositus did not exhibit any obvious clinical symptoms.

Original languageEnglish (US)
Pages (from-to)472-477
Number of pages6
JournalBBA - Protein Structure
Issue number2
StatePublished - Dec 22 1976
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)


Dive into the research topics of 'Hemoglobin Fannin-Lubbock [α2β2119(GH2) Gly → Asp]. A New Hemoglobin Variant at the α1β1 Contact'. Together they form a unique fingerprint.

Cite this