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The activation segment of procarboxypeptidase A from porcine pancreas constitutes a folded structural domain
Author(s) -
Avilés F.X.,
San Segundo B.,
Vilanova M.,
Cuchillo C.M.,
Turner C.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81112-5
Subject(s) - carboxypeptidase , circular dichroism , protein secondary structure , chemistry , trypsin , peptide , carboxypeptidase a , biochemistry , peptide sequence , protein structure , globular protein , crystallography , protein tertiary structure , biophysics , enzyme , biology , gene
The controlled action of trypsin on porcine pancreatic procarboxypeptidase A releases a large activation peptide which contains the activation segment of the proenzyme. Circular dichroism studies indicate that the isolated activation peptide contains a high percentage of residues in ordered secondary structures (mainly α‐helix). This result agrees with predictions of secondary structure carried out on the published amino acid sequence of the homologous rat proenzyme. Moreover, proton magnetic resonance spectroscopy shows that the peptide adopts a thermostable tertiary structure with characteristics typical of globular proteins. The results as a whole indicate that the activation segment of porcine pancreatic procarboxypeptidase A constitutes a folded structural domain.