Phosphate-haemoglobin interaction. The primary structure of the haemoglobin of the African elephant (Loxodonta africana, Proboscidea): asparagine in position 2 of the beta-chain.
The primary structure of the haemoglobin of the African Elephant (Loxodonta africana) is reported. The sequence was determined by means of a sequenator. The haemoglobin differs in 26 amino acids in the alpha-chains and in 27 in the beta-chains from that of adult human haemoglobin. The haemoglobin of the African Elephant, like that of the Indian Elephant and Ilama, has only 5 binding sites for polyphosphate. This finding explains the low p(O2)50 value in whole blood as a result of the lower 2,3-bisphosphoglycerate-haemoglobin interaction. This is discussed in relation to aspects of respiratory physiology; some points are also of interest with regard to the Second Punic War and Hannibal's crossing of the Alps.
D019794:2,3-Diphosphoglycerate; D000531:Altitude; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001216:Asparagine; D004163:Diphosphoglyceric Acids / Q000097:blood*; D004347:Drug Interactions; D004606:Elephants / Q000097:blood*; D006454:Hemoglobins / Q000378:metabolism; D006868:Hydrolysis; D010100:Oxygen / Q000097:blood; D011485:Protein Binding; D011487:Protein Conformation; D014357:Trypsin
D000596:Amino Acids; D004163:Diphosphoglyceric Acids; D006454:Hemoglobins; D019794:2,3-Diphosphoglycerate; D001216:Asparagine; D014357:Trypsin; D010100:Oxygen