| Literature DB >> 16789438 |
Sayit Altikat1, Abdulkadir Coban, Mehmet Ciftci, Hasan Ozdemir.
Abstract
Catalase enzyme (H202: oxidoreductase; E.C. 1.11.1.6) was purified from human skin homogenate using ammonium sulfate precipitation and DEAE-Sephadex A50 ion exchange chromatography at 4 degrees C and some characteristics of the enzyme were investigated. The human skin enzyme, having a specific activity of 1354.5 EU/mg proteins was purified with a yield of 43.13% and 1110-fold. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed a single band for the enzyme. Inhibition by piroxicam, ketoprofen, diclofenac sodium, sulfamethoxazole and nidazole occurred with I50 values of 0.414, 1.29, 1.8, 3.83, and 8.64 mM, respectively.Entities:
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Year: 2006 PMID： 16789438 DOI： 10.1080/14756360500483453
Source DB: PubMed Journal: J Enzyme Inhib Med Chem ISSN： 1475-6366 Impact factor: 5.051