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In vitro effects of some drugs on catalase purified from human skin
Authors:
Sayit Altikat a;
Abdulkadir Coban b;
Mehmet Ciftci c;
Hasan Ozdemir c
| Affiliations: | a Dumlupinar University, Nursing Training School, Kutahya, Turkey |
| b Department of Chemistry, Ataturk University, Faculty of Education, Erzincan, Turkey | |
| c Department of Chemistry, Ataturk University, Arts and Science Faculty, Erzurum, Turkey |
DOI:
10.1080/14756360500483453
Publication Frequency:
6 issues per year
Published in:
Journal of Enzyme Inhibition and Medicinal Chemistry,
Volume
21,
Issue
2
April
2006
, pages 231
- 234
Journal of Enzyme Inhibition and Medicinal Chemistry,
Volume
21,
Issue
2
April
2006
, pages 231
- 234
Subjects:
Cell Biology;
Medicinal & Pharmaceutical Chemistry;
Formats available:
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(English)
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(English)
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Abstract
Catalase enzyme (H2O2: 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°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.
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| Keywords: Catalase; Drug; Purification; Human skin; inhibition |
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