Abstract
The ratfish, Callorhynchus callorhynchus, a representative of the Holocephalii possesses a natural seric hemagglutinin characterized by a molecular weight of approximately 960.000 and composed of heavy (MW-71.200) and light (MW=23.000) polypeptides linked by disulphide bonds. Analysis of the polypeptide components, after complete reduction and alkylation, by conventional alkaline urea polyacrylamide gel electrophoresis and gel filtration on Sephadex G-200 in sodium dodecyl sulphate (SDS), did not show the presence of a J-like chain. The neutral sugar analysis of the heavy chain indicated a mannose-to-galactose ratio of 1.25. Phylogenetical implications in relation to proposed theories about the origin of the Holocephalii subclass are discussed.
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