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The primary structure of porcine pancreatic elastase. The N-terminus and disulphide bridges.

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.

SUBMITTER: Brown JR

PROVIDER: S-EPMC1270434 | biostudies-other | 1967 May

REPOSITORIES: biostudies-other

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The specificity of purified porcine pancreatic elastase.

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Amino acid sequences around the disulphide bridges and methionine residues of porcine pepsin.

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Evidence for the amino acid sequence of porcine pancreatic elastase.

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Transcriptomic profiling of murine aneurysm formation after porcine pancreatic elastase infusion

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