Phosphate-haemoglobin interaction. The primary structure of the haemoglobin of the African elephant (Loxodonta africana, Proboscidea): asparagine in position 2 of the beta-chain

Abstract

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.