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A protease active with N-alpha-benzoyl-DL-arginine-p-nitroanilide with an optimum pH of 7.3 has been found in the cytosol of rat liver. The activity of this protease increased in N-2-fluorenylacetamide-induced hepatoma as well as in fetal liver. It has been purified from normal liver and hepatoma about 200-fold. Its molecular weight is estimated by gel filtration to be about 200,000 in each tissue. The protease activity is unaffected by chymostatin, pepstatin, soybean trypsin inhibitor, and p-chloromercuribenzoate. Antipain, leupeptin, tosyl-L-lysine chloromethyl ketone, and phenylmethylsulfonyl fluoride inhibit the protease activity. This protease appears to be a serine protease.
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K Wada, and
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K Wada, and
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October 1972,
Cancer research,
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K Wada, and
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K Wada, and
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K Wada, and
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July 1982,
Journal of the National Cancer Institute,
K Wada, and
H Matsui, and
K Tsukada
August 1965,
Cancer research,
