Homeothermic Fish and Hemoglobin: Primary Structure of the Hemoglobin from Bluefin Tuna(Thunnus thynnus,Scromboidei)

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Abstract
Some fish are warm-bodied, e.g. the bluefin tuna (Thunnus thynnus), which has a muscle temperature 12-17.degree. C higher than its environment. This endothermy is achieved by aerobic metabolism and conserved by means of a heat-exchanger system. The hemoglobins of bluefin tuna are adapted to these conditions by their endothermic oxygenation, thus contributing to the preservation of the body energy. This is a new and so far unique property of tuna hemoglobin. The primary structure of the .alpha. and .beta. chains of bluefin tuna hemoglobins is presented. The sequence was determined after enzymatic and chemical cleavages of the chains and sequencing of the peptides in gas- and liquid-phase sequencers. The .alpha. chains consists of 143 residues and are N-terminally acetylated. The .beta. chains have 146 amino acids and show two ambiguities at positions 140 and 142. The .alpha. chains differ from the human .alpha. chains in 65 amino-acid residues, the .beta. chains in 76. The hemoglobins of bluefin tuna, carp and man are compared and their different physiological properties are discussed in relation to the sequence data. From the primary structure of tuna hemoglobins, it is possible to propose a molecular basis for their peculiar endothermic transition from the T to the R structure.

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