Studies on yak hemoglobin (Bos grunniens, Bovidae): structural basis for high intrinsic oxygen affinity?

Biol Chem Hoppe Seyler. 1985 Jan;366(1):63-8. doi: 10.1515/bchm3.1985.366.1.63.

Abstract

Two types of alpha- and two types of beta-chains are found in the hemoglobin of yak population. The complete amino-acid sequences of the four polypeptide chains were determined. The two alpha-chains differ by two and the two beta-chains by three amino-acid substitutions. The substitution of valine at position 135 in the beta II-chain may be responsible for the high intrinsic oxygen affinity of yak hemoglobin.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Cattle / blood*
  • Cyanogen Bromide
  • Electrophoresis, Polyacrylamide Gel
  • Globins / analysis
  • Hemoglobins / analysis*
  • Hydrolysis
  • Oxygen / blood*
  • Peptides / analysis
  • Trypsin

Substances

  • Amino Acids
  • Hemoglobins
  • Peptides
  • Globins
  • Trypsin
  • Cyanogen Bromide
  • Oxygen