Abstract
The complete amino acid sequence of a biologically and immunologically active fragment, Fr. AA-1, of salivary gland hormone (parotin) has been established through the uses of combined dansyl-Edman procedure, manual Edman degradation and standard enzymatic and chemical techniques. The binding site of the carbchydrate moiety was determined from the amino acid composition of the carbohydrate moiety obtained from digests of Fr. AA-1 with pronase. Fr. AA-1 was shown to be a glycopeptide consisting of 58 amino acid residues. Its sequence is : H2N-Leu^^1-Tyr-Ile-Leu-Tyr-Phe-Phe-Gln-Ser-Asp^^10-Asn-Glu-Asp-Lys-Glu-Lys-Val-Val-Arg-Gln^^20-Glu-Glu-Gly-Glu-Glu-Arg-Ile-Thr-Ala-Leu^^30-Leu-Met-Asn (carbohydrate moiety)-Gly-Ser-Ala-Leu-Lys-Gln-Glu^^40-Glu-Trp-Trp-Glu-Gly-Lys-Glu-Asp-Thr-Asp^^50-Asp-Thr-Ala-Ile-Val-Leu-Leu-Lys^^58-COOH.
