Monkey pepsinogens and pepsins. IV. The amino acid sequence of the activation peptide segment of Japanese monkey pepsinogen.

The complete amino acid sequence of the activation peptide segment of the major component of Japanese monkey pepsinogens was determined. The pepsinogen was converted to pepsin by incubation at pH 2.0 and 14 degrees C for 17 min. The activation peptides were separated from the resulting pepsin and purified by chromatography on columns of sulfopropyl (SP)-Sephadex. One 25-residue peptide and two 22-residue peptides were isolated and their amino acid sequences were determined. The results showed that the former peptide was derived from the amino-terminal half (residues no. 1 to 25) and the latter peptides from the carboxyl-terminal half (residues no. 26 to 47) of the activation segment. The latter two peptides were identical except for a single amino acid replacement. The complete amino acid sequence of the whole activation peptide segment was thus deduced as follows: Ile1-Ile-Tyr-Lys-Val-Pro-Leu-Val-Arg-Lys10-Lys-Ser-Leu-Arg-Arg-Asn-Leu-Ser-Glu- His20-Gly-Leu-Leu-Lys-Asp-Phe-Leu-Lys-Lys-His30-Asn-Leu-Asn-Pro-Ala-Ser-Lys-Tyr -Phe-Pro40-LysGln-Ala-Glu-Ala-Pro-Thr-Leu47. The whole chain was composed of 47 residues, and cleaved into two polypeptides by the cleavage of Asp25-Phe26 bond during activation. Two amino acids were detected at residue-41, i.e., glutamine and lysine, indicating the presence of two closely related pepsinogens in the sample used. The total number of residues (47) of the whole activation peptide segment is 3 and 2 residues larger than those of porcine pepsinogen and bovine pepsinogen, respectively. The differences are 15 and 22 residues as compared with porcine pepsinogen and bovine pepsignogen, respectively.