ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Different proteases were isolated and purified from viscera of surf clam, Spisula solidissima. These proteases were similar to cathepsins D and B, with molecular weights of −36,700 and −17,400 daltons, respectively. Optimum activity of enzymes towards hemoglobin and casein occurred from pH 2.5–3.0 and temperature 44–46°C. Cathepsin D-like protease, a carboxyl protease, was insensitive to most protease inactivators, but extremely sensitive to pepstatin. Cathepsin B-like protease, a thiol protease, was activated by thiol-reducing agents and metal chelators, but was sensitive to many reagents such as iodoacetamide, Tosyl-phenylalanine chloromethyl ketone, Tosyl-lysine chloromethyl ketone, phenylmethanesulphonyl fluoride, leupeptin and heavy metals.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1986.tb10838.x
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