title: Aminopeptidase activities present in tissues of Helix aspersa.
abstract: 1. Tissues of Helix aspersa have been examined for the presence of aminopeptidase activities. 2. Enzyme activities were detected using synthetic peptide substrates containing the fluorescent leaving group 7-amino-4-methyl coumarin. The methods used included continuous fluorimetric assay and activity staining of enzymes in non-denaturing polyacrylamide gels. 3. Several types of peptidase activity were detected, including three distinct aminopeptidases which differ in molecular size and substrate preference.
authors.affiliation: Division of Biochemistry, School of Biology and Biochemistry, Queen's University, Belfast, UK.
authors.forename: M P
authors.initials: MP
authors.lastname: Ennis
authors.forename: G B
authors.initials: GB
authors.lastname: Irvine
authors.forename: C H
authors.initials: CH
authors.lastname: Williams
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D006372:Helix, Snails / Q000201:enzymology*; D008969:Molecular Sequence Data; D009842:Oligopeptides; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
chemical_list: D009842:Oligopeptides; D000626:Aminopeptidases