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Science 25 November 1966:
Vol. 154. no. 3752, pp. 1024 - 1027
DOI: 10.1126/science.154.3752.1024
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Articles

Hemoglobin Freiburg: Abnormal Hemoglobin Due to Deletion of a Single Amino Acid Residue

R. T. Jones 1, B. Brimhall 1, T. H. J. Huisman 2, E. Kleihauer 3, and K. Betke 3

1 Division of Experimental Medicine and Department of Biochemistry, University of Oregon Medical School, Portland
2 Department of Biochemistry, Medical College of Georgia, Augusta
3 Universitäts-Kinderklinik, Tübingen, Germany

Structural characterization of a new variant of human hemoglobin (adult), designated hemoglobin Freiburg, indicates the deletion of the valyl residue No. 23 from an otherwise normal beta-chain. The formula may be written agr2beta223val—0. The abnormal hemoglobin is present with hemoglobin A in the proposita and in two of her three living children, but is not detectable in her parents. We postulate that this variant represents a triplet base deletion which most likely resulted from an unequal crossing-over between two normal betachain loci during meiosis in one of the parents of the proposita.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Hemoglobin Gun Hill: Deletion of Five Amino Acid Residues and Impaired Heme-Globin Binding.
T. B. Bradley Jr., R. C. Wohl, and R. F. Rieder (1967)
Science 157, 1581-1583
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Science. ISSN 0036-8075 (print), 1095-9203 (online)