Abstract
An enzyme which catalyzes the conversion of intraprotein arginine residue to intraprotein citrulline residue is present in bovine snout epidermis. This arginine-converting enzyme has been partially purified by (NH 4) 2SO 4 preciptation chromatography on DEAE-cellulose and chromatography on Sephadex G-200. The enzyme is active at neutral pH, requires Ca 2+ and a reducing agent and has an apparent molecular weight of 69 000. Its substrates include histone, polyarginine, S- carboxymethyl cysteine-hair keratin, S- carboxymethyl cysteine epidermal keratin and prekeratin and S- carboxymethyl cysteine-trichohyalin. A large number of proteins, synthetic and naturally occurring peptides, and other guanidine-containing compounds were not substrates of the arginine-converting enzyme.
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