Abstract
In media containing proteins as the nitrogen source some strains of Candida albicans excrete proteolytic enzymes with an optimum of activity at pH 3.2. A 140-fold purification of the enzyme from one of these strains was achieved by gel filtration and chromatography on DEAE-Sephadex. The molecular weight of the protein was found to be 40 000; the frictional ratio, 1.3. The proteolytic activity was not influenced by the addition of heavy metal ions, SH-blocking reagents, p-bromophenacyl bromide, N-diazoacetylnorleucine methyl ester, or various inorganic ions. Cleavage of oxidized insulin β-chain and albumin demonstrated a low side-chain specificity; a preferential attack, on hydrophobic amino acid residues was observed after incubation for short periods of time.
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