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  • Title: Amino-acid sequence of porcine pepsin.
    Author: Tang J, Sepulveda P, Marciniszyn J, Chen KC, Huang WY, Tao N, Liu D, Lanier JP.
    Journal: Proc Natl Acad Sci U S A; 1973 Dec; 70(12):3437-9. PubMed ID: 4587252.
    Abstract:
    As the culmination of several years of experiments, we propose a complete amino-acid sequence for porcine pepsin, an enzyme containing 327 amino-acid residues in a single polypeptide chain. In the sequence determination, the enzyme was treated with cyanogen bromide. Five resulting fragments were purified. The amino-acid sequence of four of the fragments accounted for 290 residues. Because the structure of a 37-residue carboxyl-terminal fragment was already known, it was not studied. The alignment of these fragments was determined from the sequence of methionyl-peptides we had previously reported. We also discovered the locations of activesite aspartyl residues, as well as the pairing of the three disulfide bridges. A minor component of commercial crystalline pepsin was found to contain two extra amino-acid residues, Ala-Leu-, at the amino-terminus of the molecule. This minor component was apparently derived from a different site of cleavage during the activation of porcine pepsinogen.
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