Phosphate-Haemoglobin Interaction. The Primary Structure of the Haemoglobin of the African Elephant(Loxodonta africana,Proboscidea): Asparagine in Position 2 of the β-Chain
- 1 January 1984
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 365 (2), 743-750
- https://doi.org/10.1515/bchm2.1984.365.2.743
Abstract
The primary structure of the Hb of the African elephant (L. africana) is reported. The sequence was determined by means of a sequenator. The Hb differs in 26 amino acids in the .alpha.-chains and in 27 in the .beta.-chains from that of adult human Hb. The Hb of the African elephant, like that of the Indian elephant and llama, has only 5 binding sites for polyphosphate. This finding explains the low P(O2)50 [O2 tension at 1/2 Hb saturation] value in whole blood as a result of the lower 2,3-bisphosphoglycerate-Hb interaction. This is discussed in relation to aspects of respiratory physiology.This publication has 15 references indexed in Scilit:
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