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- W2016011502 abstract "Four proteases (CP-I, -II, -111 and -IV) were isolated and purified from hepatopancreas of crawfish. Based upon their activities with known inhibitors, they resembled trypsin. All were cross-reactive with polyclonal antibodies raised against CP-II, indicating they shared structural components. Each of these was able to inactivate orange peel pectinesterase, tomato pectinesterase and pectate lyase C at room temperature under nondenaturing conditions. Using matrix-assisted-laser-desorption time of flight mass spectrometry (MALDl-TOF MS), an analysis of peptides generated during proteolysis of pectate lyase C from Erwinia chrysenthemi showed similar peptide patterns for the four crawfish proteases, indicating a common specificity for each isozyme. However, the cleavage patterns were different from those obtained by the action of bovine trypsin on pectate lyase C. These studies indicate the four proteases from the hepatopancreas of crawfish are isozymes which may be used for the inactivation of pectinolytic enzymes." @default.
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- W2016011502 date "2001-09-01" @default.
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- W2016011502 title "THE EFFECT OF CRAWFISH PROTEASES ON INACTIVATION AND THE HYDROLYTIC CLEAVAGE OF PECTIC ENZYMES" @default.
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- W2016011502 doi "https://doi.org/10.1111/j.1745-4514.2001.tb00743.x" @default.
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