Abstract

A high-molecular parotin -active substance, E-3, was isolated by zone electrophoresis, using Pevikon as the supporting agent, from the fraction possessing a parotin-like activity obtained from the Pronase digest of saliva-parotin-A. This E -3 contained 31.33% of amino acid residue, rich in the content of proline and glutamic acid. The N-terminal amino acid was not detected by the DNP method, while C-terminal was proved to be serine by hydrazine decomposition. E-3 contains sugars consisting of 30.16% of hexose residue and 11.25% of hexosamine residue, and does not contain uronic and sialic acids. E-3 also contains 26.80% of lipid which was assumed to be a glycolipid from its qualitative estimation. Isoelectric point measured by electrophoresis on cellulose acetate was at pH.4.4, and the molecular weight of E-3 measured by the Archibald method was 55000, agreeing with the value calculated from the content of amino acid residue.

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