| Literature DB >> 6626147 |
T Namikawa, O Takenaka, K Takahashi.
Abstract
The structure of the beta chain of adult bovine hemoglobin Bali of the Bali cattle was determined and compared to those of beta A, beta B, and other beta-chain variants of domestic cattle reported previously. The lysine residue at beta A18 was substituted by histidine in beta Bali18. This change requires two base substitutions at the codon and is also found in beta B18. The beta B chain differs from the beta A chain at residue Nos. 15, 18, and 119. It was concluded that a common ancestor of the beta B and beta Bali first diverged from the beta A chain through the Lys leads to His substitution. This fact indicates that the high degree of dimorphism of the beta A and beta B chains in Indian humped cattle is a result of its hybrid origin. An evolutionary tree for the bovine hemoglobin beta-chain variants was constructed based on parsimonious evolution and homology with related species.Entities:
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Year: 1983 PMID: 6626147 DOI: 10.1007/bf00498925
Source DB: PubMed Journal: Biochem Genet ISSN: 0006-2928 Impact factor: 1.890