Preliminary studies on haemoglobin and other proteins of the Pogonophora
1966
Manwell, C. | Southward, E.C. | Southward, A.J.
Starch gel electrophoresis of extracts of Siboglinum atlanticum showed that all five individuals tested have two acidic haemoglobin components and a strong a-naphthyl acetate esterase. There was individual variation in the position of the esterase. Low levels of amylase activity were found in the extracts but no trace of dehydrogenases for such important substrates as glucose-6-phosphate, lactate, malate, and glutamate could be revealed by standard histochemical methods as applied to zone electrophoresis. The high level of haemoglobin and the protein peculiarities of the Pogonophora are discussed in relation to experiments on respiration. It is concluded that Siboglinum haemoglobin functions at very low oxygen partial pressures and that the high level of haemoglobindissolved in the blood plasma of pogonophores does not reflect a high level of oxygen consumption or activity. The meagre biochemical data at present available on the Pogonophora do not favour relationship of this phylum to the echinoderm-chordate line any more than to the annelids or other invertebrate phyla.
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