title: Characterization of fish acid proteases by substrate-gel electrophoresis.
abstract: Several analytical techniques based upon the use of substrate-polyacrylamide gel electrophoresis were evaluated to achieve characterization of aspartate proteases in fish stomach. Since aspartate proteases of fish are more stable at high pH than mammalian pepsins, the most accurate technique for activity assessment is electrophoresis at neutral pH and revealing of such activity at low pH with hemoglobin as substrate. The technique is suitable for characterization of proteases and in comparative assessment of acid protease activity in different sparids.
authors.affiliation: Departamento Biología Aplicada, Universidad de Almería, Spain. mdiaz@ualm.es
authors.forename: M
authors.initials: M
authors.lastname: Díaz-López
authors.forename: F J
authors.initials: FJ
authors.lastname: Moyano-López
authors.forename: F J
authors.initials: FJ
authors.lastname: Alarcón-López
authors.forename: F L
authors.initials: FL
authors.lastname: García-Carreño
authors.forename: M A
authors.initials: MA
authors.lastname: Navarrete del Toro
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005399:Fishes / Q000378:metabolism*; D005753:Gastric Mucosa / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D010473:Perciformes / Q000378:metabolism; D013379:Substrate Specificity