Über den Einfluß von Oxydations- und Reduktionsmitteln auf die Aktivität von Papain.

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Abstract
Papain partially inactivated by oxidation responded in decreasing intensity to additions of 0.002 M gluta-thione, thioglycolic and thiolactic acids, respectively. Halogen acetic acids inhibited activator-free papain, indicating reaction with a prosthetic group directly rather than with SH activators. 0.001 M iodoacetic and bromo-acetic acids were strongly inhibitory, while chloroacetic acid had but little inhibitory activity. SH compounds partially restored the activity of the iodoacetic acid-treated enzyme. Iodoacetic and selenite inhibitions were synergistic. Cyano- and azidoacetic acids did not inhibit either partially inactive nor thioglycolic-acid-treated papain. Tellurite and pilocarpine had little or no inhibitory activity; iodin and quinone completely inhibited papain. Diazomethane reduced the activity by half. Papain completely inactivated by peroxide recovered only part of its activity on treatment with H2S or hydroquinone, but all on treatment with glutathione, sulfite or a dehydrogenase-succinate system. Dehy-drogenase-fumarate brought about a slight inactivation. Failure to purify papain might be interpreted as in-creasing the sensitivity to oxidation by removing redox buffers in the previous purification processes.

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