title: Digestive proteinases of Artemesia longinaris (Decapoda, Penaeidae) and relationship with molting.
abstract: Digestive proteinase activities of Artemesia longinaris were assayed at different stages of the molting cycle. Total proteolytic activity in the hepatopancreas was highest during postmolt. Trypsin and chymotrypsin activities were highest during intermolt. Specific inhibitors and zymograms of A. longinaris hepatopancreas extracts showed four trypsins (14.79, 15.49, 16.60, 17.38 kDa, respectively) and three chymotrypsins (21.38, 22.91, 27.54 kDa, respectively). Our results suggest that proteolytic activity in the hepatopancreas of A. longinaris is influenced by the molting cycle. Types and activity of prawn digestive enzymes constitute background information to further study the digestive abilities of these organisms and will lead to understanding their nutritional needs and feeding ecology.
authors.affiliation: Departamento Ciencias Marinas, Facultad Ciencias Exactas y Naturales, CONICET, Universidad Nacional de Mar del Plata, Funes 3350, B7602AYL, Mar del Plata, Argentina.
authors.forename: A V
authors.initials: AV
authors.lastname: Fernández Gimenez
authors.forename: F L
authors.initials: FL
authors.lastname: García-Carreño
authors.forename: M A
authors.initials: MA
authors.lastname: Navarrete del Toro
authors.forename: J L
authors.initials: JL
authors.lastname: Fenucci
mesh_terms: D000818:Animals; D002918:Chymotrypsin / Q000737:chemistry / Q000378:metabolism; D033364:Decapoda / Q000201:enzymology* / Q000502:physiology*; D004064:Digestive System / Q000201:enzymology*; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D018978:Molting / Q000502:physiology*; D011480:Protease Inhibitors / Q000494:pharmacology; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism
chemical_list: D011480:Protease Inhibitors; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin