首页|PROTEASES FROM PENAEUS MONODON FABRICIUS, 1798 (DECAPODA, PENAEIDAE): PARTIAL CHARACTERIZATION AND LOCALIZATION
PROTEASES FROM PENAEUS MONODON FABRICIUS, 1798 (DECAPODA, PENAEIDAE): PARTIAL CHARACTERIZATION AND LOCALIZATION
扫码查看
点击上方二维码区域，可以放大扫码查看
原文链接
NSTL
Brill
This study aimed to characterize and determine the distribution of proteases in various anatomical parts of Penaeus monodon using mainly electrophoresis on sodium dodecyl sulfate (SDS) polyacry-lamide gels impregnated with casein (casein-SDS-PAGE) and specific protease inhibitors. Twelve caseinolytic bands designated A-L, with estimated molecular masses of 11.4-49.6 kDa were detected by SDS-PAGE, and were most abundant in the hepatopancreas. Among the 12 bands, E, J, K and L were predominant, A, G and H were identified as chymotrypsin-like proteases, D, E, I, J, K and L were identified as trypsin-like proteases, and B, C and F were identified as serine proteases. The proteases were most active at 50 degrees C and pH 7.0. The proteolytic and trypsin-like activities of Penaeus monodon were most abundant in hepatopancreas extracts and least abundant in extracts from the haemolymph. Trypsin-like proteases in the hepatopancreas extract were found to activate prophe-noloxidase (proPO) to form phenoloxidase (PO).
NSTL
Brill
