Purification and characterization of the protease inhibitor "monastatin" from a marine Alteromonas sp. with reference to inhibition of the protease produced by a bacterium pathogenic to fish

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Abstract
A novel protease inhibitor, which we named "monastatin," produced by a marine bacterium was purified using ammonium sulfate precipitation, DEAE-cellulofine column chromatography, and gel filtration through Sephadex G-100. Monastatin was purified to homogeneity, as a single staining band in polyacrylamide gel electrophoresis. Monastatin was a glycoprotein with a molecular weight of about 20 000. It was stable up to 100.degree. C for a 30-min incubation with loss of 20% of inhibitory activity and also showed stability over a wide range of pH from 2 to 12. Metal ions such as Cu2+ and Fe2+ repressed the inhibitory activity to 0%. Monastatin had an inhibitory activity against thiol proteases such as papain and ficin.

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