Aminopeptidase activities present in tissues of Helix aspersa.
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.
Ennis
M P
MP
Division of Biochemistry, School of Biology and Biochemistry, Queen's University, Belfast, UK.
Irvine
G B
GB
Williams
C H
CH
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
D009842:Oligopeptides; D000626:Aminopeptidases