title: Acid proteinase activity in fish--I. Comparative study of extraction of cathepsins B and D from Mujil auratus.
abstract: Acid catheptic activity was measured in crude extracts of muscle, liver, heart, spleen and gonads from the fishes Mujil auratus, Sparus aurata and Lightonatus mormyrus. The spleen was the organ which showed the highest activity. A comparative study of the seven most commonly used extraction methods was made. Some were modified to account for the characteristics of the fish organs and the activity extracted from them. The Siebert method resulted as the best extraction method only if 1 mM EDTA was present in the medium. The activity from Mujil auratus muscle was strongly inhibited by iodoacetate, N-ethylmaleimide, p-hydroxy mercuribenzoate, and diazo-acetyl-DL-norleucine methyl ester. The results indicated the presence of a carboxyl-proteinase and a thiol-proteinase. According to inhibition studies, the levels of proteinase and amidase activities shown by different organs of Mujil auratus were re-examined. The spleen extract showed the maximum activity for both cathepsins, but muscle extract accounted for more than 95% of total catheptic activity.
mesh_terms: D000818:Animals; D002401:Cathepsin B; D002402:Cathepsin D; D002403:Cathepsins / Q000302:isolation & purification*; D005399:Fishes / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D011480:Protease Inhibitors / Q000494:pharmacology; D013045:Species Specificity; D013154:Spleen / Q000201:enzymology; D014018:Tissue Distribution
chemical_list: D011480:Protease Inhibitors; D002403:Cathepsins; D002401:Cathepsin B; D002402:Cathepsin D