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. 1973 Dec;70(12 Pt 1-2):3437–3439. doi: 10.1073/pnas.70.12.3437

Amino-Acid Sequence of Porcine Pepsin

J Tang 1,2, P Sepulveda 1,2, J Marciniszyn Jr 1,2, K C S Chen 1,2,*, W-Y Huang 1,2,†, N Tao 1,2,*, D Liu 1,2, J P Lanier 1,2
PMCID: PMC427253  PMID: 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.

Keywords: protein, cyanogen bromide, active site

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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