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Monkey pepsinogens and pepsins. 7. Analysis of the activation process and determination of the NH2-terminal 60-residue sequence of Japanese monkey progastricsin, and molecular evolution of pepsinogens


Monkey pepsinogens and pepsins. 7. Analysis of the activation process and determination of the NH2-terminal 60-residue sequence of Japanese monkey progastricsin, and molecular evolution of pepsinogens



Journal of Biochemistry (Tokyo): 974: 1235-1246



Japanese monkey progastricsin was shown to be activated to gastricsin exclusively by a 2-step process through an intermediate form. The occurrence of this process was substantiated by the isolation of the intermediate form and released peptides. By NH2-terminal sequence analyses of these protein and peptide species, the amino acid sequence of the 43-residue activation (propart) was determined to be as follows: Ala-Val-Val-Lys-Val-Pro-Leu-Lys-Lys-Phe-Lys-Ser-Ile-Arg-Glu-Thr-Met-Lys-Glu-Lys-Gly-Leu-Leu-Gly-Glu-Phe-Leu-Arg-Thr-His-Lys-Tyr-Asp-Pro-Ala-Trp-Lys-Tyr-His-Phe-Gly-Asp-Leu. The NH2-terminal 26-residue peptide was released first, resulting in generation of the intermediate form. The subsequent release of peptide residues, 27-40 and 27-43, generated 2 gastricsins as the final products. This 2-step process of activation of Japanese monkey progastricsin is in striking contrast to the 1-step activation process occurring exclusively for pepsinogen A of the same monkey species. The course of molecular evolution of pepsinogens including progastricsins was deduced from the amino acid sequences of their activation segments by constructing phylogenic trees. The trees divided pepsinogens into 3 clusters, i.e., pepsinogens A, progastricsins and prochymosin, showing that these 3 groups diverged from one another very early on in the course of the evolution of pepsinogens.

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Related references

Monkey pepsinogens and pepsins. VII. Analysis of the activation process and determination of the NH2-terminal 60-residue sequence of Japanese monkey progastricsin, and molecular evolution of pepsinogens. Journal of Biochemistry 97(4): 1235-1246, 1985

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