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Science 23 September 1966:
Vol. 153. no. 3743, pp. 1539 - 1543
DOI: 10.1126/science.153.3743.1539
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Articles

Hemoglobins in Sheep: Multiple Differences in Amino Acid Sequences of Three Beta-Chains and Possible Origins

Samuel H. Boyer 1, Peter Hathaway 1, Flora Pascasio 1, Charlene Orton 1, James Bordley 1, and Michael A. Naughton 2

1 Division of Medical Genetics, Johns Hopkins Hospital and University School of Medicine, Baltimore, Maryland
2 Department of Biophysics, Johns Hopkins University School of Medicine

Among the three adult sheep hemoglobins (A, B, and C), two (A and B) are reportedly products of alleles. The beta-chains of A and B differ by at least seven scattered amino acid residues whereas the beta-sequence of C differs from A by at least 16 residues and from B by at least 21 residues. These changes suggest that the origin of C-beta antedated the divergence of A and B. Five shared differences between A-beta and C-beta with respect to B-beta can be interpreted as the result of selective advantage in favor of B. A complex of additional mechanisms has possibly been involved in maintaining the A-B- C porymorphism.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Activation of Hemoglobin C Synthesis in Sheep Marrow Culture.
J. W. Adamson and G. Stamatoyannopoulos (1973)
Science 180, 310-312
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Gene Selection in Hemoglobin and in Antibody-Synthesizing Cells.
D. Kabat (1972)
Science 175, 134-140
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Silent Hemoglobin Alpha Genes in Apes: Potential Source of Thalassemia.
S. H. Boyer, A. N. Noyes, G. R. Vrablik, L. J. Donaldson, E. W. Schaefer Jr., C. W. Gray, and T. F. Thurmon (1971)
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Immunoglobulin Structure: Variation in Amino Acid Sequence and Length of Human Lambda Light Chains.
F. W. Putnam, T. Shinoda, K. Titani, and M. Wikler (1967)
Science 157, 1050-1053
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