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. 1967 May;103(2):497–507. doi: 10.1042/bj1030497

The primary structure of porcine pancreatic elastase

The N-terminus and disulphide bridges

J R Brown 1, Dorothy L Kauffman 1, B S Hartley 1
PMCID: PMC1270434  PMID: 5340368

Abstract

1. The amino acid composition and N-terminal groups of purified elastase show that it is a single peptide chain of 234 residues. 2. The N-terminal sequence is Val-Val-Gly-Gly-Thr-Glu-. 3. The sequences around the four disulphide bridges were determined by using a `diagonal' electrophoretic technique. 4. These four bridges are homologous with the four common to bovine trypsin and chymotrypsin. 5. Out of 83 residues of the elastase sequence so far determined, 43 are homologous with similar regions of trypsin and chymotrypsin. 6. The evolutionary ancestry of these enzymes is discussed.

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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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