Studies on yak hemoglobin (Bos grunniens, Bovidae): structural basis for high intrinsic oxygen affinity?
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle / Q000097:blood*; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005914:Globins / Q000032:analysis; D006454:Hemoglobins / Q000032:analysis*; D006868:Hydrolysis; D010100:Oxygen / Q000097:blood*; D010455:Peptides / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D006454:Hemoglobins; D010455:Peptides; D005914:Globins; D014357:Trypsin; D003488:Cyanogen Bromide; D010100:Oxygen