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Inhibition of Peroxidase, Trypsin, and alpha-Chymotrypsin by Platinum (II) and Platinum (IV) Complexes

S. V. Muginova1, E. V. Vil'ms1, T. N. Shekhovtsova1*, and V. B. Ivanov2

1School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-4675

2Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Botanicheskaya ul. 35, Moscow, 127276 Russia

* To whom correspondence should be addressed.

Received June 5, 1998; Revision received July 10, 1998
Effects of various complexes of platinum (II) and platinum (IV) on activities of trypsin, alpha-chymotrypsin, and peroxidase were compared. The platinum (II) complexes were found to inhibit these enzymes, though with variable efficiency. The platinum (IV) complexes at concentrations <= 0.2 mM efficiently inhibited peroxidase but had no effect on the proteases. An enzymatic assay was developed to measure the most effective peroxidase inhibitor (cisplatin) at concentrations of 5-50 µM in the presence of fivefold excess of its isomer (transplatin).
KEY WORDS: peroxidase, trypsin, alpha-chymotrypsin, platinum-containing inhibitors