Collect. Czech. Chem. Commun.
1979, 44, 2284-2292
https://doi.org/10.1135/cccc19792284
Primary structure of peptides which form the disulfide bonds of chicken pepsin
Helena Keilová, Miroslav Baudyš and Vladimír Kostka
Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6
Abstract
The molecule of chicken pepsin is cross-linked by three disulfide bonds. The structures of the half-cystine peptides which form these bonds were determined by the analysis of different enzymic digests of the enzyme. The order of the disulfide bonds in the molecule was elucidated with regard to sequential homologies between chicken pepsin and other acid proteases. The three disulfide bonds of chicken pepsin, numbered from the N-terminus of pepsin, are: 1st bond Ile-Tyr-Cys-(Lys-Ser-Ser-Ala)-Cys-Ser-Asn-His-Lys; 2nd bond Val-Ala-Cys-Cys-(Thr-Phe)-Gln-Ala; 3rd bond Asp-Leu-Gly-Val-Ser-Ser-Asp-Gly-Glu-Ile-Ser-Cys-(Asp-Asp-Ile-Ser-Lys-Leu-Pro-Asp)-Cys-(Ser-Gly-Asp-Glu-Asn-Leu-Val)-Met.
