The digestive proteases of langostilla (pleuroncodes planipes,decapoda): their partial characterization,and the effect of feed on their composition |
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Affiliation: | 1. Biology Centre of the Czech Academy of Sciences, Institute of Hydrobiology, Na Sádkách 7, 370 05 České Budějovice, Czech Republic;2. University of South Bohemia, Faculty of Science, Branišovská 31, 370 05 České Budějovice, Czech Republic |
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Abstract: | - 1.1. Three methods of recuperating and preserving enzyme activity from freshly-caught langostilla were assessed. In the pressing and acetone extract methods, the recovered specific activity was similar.
- 2.2. Protease activity was higher between 6.5 and 8 pH, and was sensitive to high temperatures.
- 3.3. In PAGE and serine inhibition assays, one fraction resembled bovine trypsin.
- 4.4. The composition of proteins and molecules bearing protease activity from the hepatopancreas and stomach of both fed and starved animals was similar, indicating proteases are not induced but constitutive.
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