Abstract
Several proteases were found in an aqueous extract from the hepatopancreas of blue abalone. Four, called PH1, PH2, PH3 and PH4, were purified by ammonium sulfate precipitation, low pressure DEAE-Sepharose chromatography and anion exchange HPLC. All these proteases were active on protein substrates (casein and hide powder azure); they showed different activities with synthetic substrates and were inhibited by different compounds. PH1, PH2 and PH3 seemed to be serine-like proteases (PH1, chymotrypsin-like; PH2 and PH3, trypsin-like) while protease PH4 had carboxypeptidase behavior. The purified enzymes showed single bands in SDS-PAGE and IEF minigels showing relative molecular masses of 28,100, 29,500, 32,000 and 30,000, and isoelectric points of 6.3, 3.6, 4.0 and 3.8, respectively. PH1, PH2 and PH3 have common features in their amino acid contents. These enzymes possess different secondary structures as judged from their circular dichroism spectra.
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