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Hemoglobin Bali (bovine): βA18(Bl)Lys → his: One of the “missing links” between βA and βB of domestic cattle exists in the Bali cattle (Bovinae, Bos banteng)

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Abstract

The structure of the β chain of adult bovine hemoglobin Bali of the Bali cattle was determined and compared to those of βA, βB, and other β-chain variants of domestic cattle reported previously. The lysine residue at βA 18 was substituted by histidine in βBali 18. This change requires two base substitutions at the codon and is also found in βB 18. The βB chain differs from the βA chain at residue Nos. 15, 18, and 119. It was concluded that a common ancestor of the βB and βBali first diverged from the βA chain through the Lys → His substitution. This fact indicates that the high degree of dimorphism of the βA and βB chains in Indian humped cattle is a result of its hybrid origin. An evolutionary tree for the bovine hemoglobin β-chain variants was constructed based on parsimonious evolution and homology with related species.

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Authors and Affiliations

  1. Laboratory of Animal Genetics, Faculty of Agriculture, Nagoya University, Chikusa-ku, 464, Nagoya, Japan

    Takao Namikawa

  2. Department of Biochemistry, Primate Research Institute, Kyoto University, 484, Inuyama, Aichi, Japan

    Osamu Takenaka & Kenji Takahashi

Authors
  1. Takao Namikawa
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  2. Osamu Takenaka
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  3. Kenji Takahashi
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This work was supported in part by Grants-in-Aid for Overseas Scientific Survey of Ministry of Education, Science and Culture, Japan (304115 and 404315).

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Namikawa, T., Takenaka, O. & Takahashi, K. Hemoglobin Bali (bovine): βA18(Bl)Lys → his: One of the “missing links” between βA and βB of domestic cattle exists in the Bali cattle (Bovinae, Bos banteng). Biochem Genet 21, 787–796 (1983). https://doi.org/10.1007/BF00498925

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  • DOI: https://doi.org/10.1007/BF00498925

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