Primary structure of the hemoglobin beta-chain of rose-ringed parakeet (Psittacula krameri)

J Protein Chem. 1989 Aug;8(4):481-6. doi: 10.1007/BF01026432.

Abstract

The primary structure of Rose-ringed Parakeet hemoglobin beta-chain was established, completing the analysis of this hemoglobin. Comparison with other avian beta-chains show variations smaller than those for the corresponding alpha-chains. There are 11 amino acid exchanges in relationship to the only other characterized psittaciform beta-chain, and a total of 35 positions are affected by differences among all avian beta-chains analyzed (versus 61 for the alpha-chains). At three positions, the Psittacula beta-chain has residues unique to this species. Three alpha 1 beta 1 contacts are modified, by substitutions at positions beta 51, beta 116, and beta 125.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Hemoglobins / analysis*
  • Hemoglobins / isolation & purification
  • Molecular Sequence Data
  • Parakeets / blood*
  • Psittaciformes / blood*
  • Species Specificity

Substances

  • Hemoglobins