In vitro effects of some drugs on catalase purified from human skin
ArticleAçık Erişim
Özet
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 I 50 values of 0.414, 1.29, 1.8, 3.83, and 8.64 mM, respectively. © 2006 Taylor & Francis.
Anahtar Kelimeler
CatalaseDrugHuman skinInhibitionPurificationAnti-Inflammatory Agents, Non-SteroidalDiclofenacDose-Response Relationship, DrugEnzyme InhibitorsHumansInhibitory Concentration 50KetoprofenPiroxicamSkinSulfamethoxazoleammonium sulfatemetronidazolearticleconcentration responsecontrolled studydrug mechanismenzyme analysisenzyme inhibitionenzyme purificationenzyme specificityhumanhuman tissueIC 50in vitro studyinhibition kinetics
RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/ebyu/16042Resmi atıflarda kullanılan kalıcı adresTam Kayıt
| Alan | Değer | Dil |
|---|---|---|
| dc.contributor.author | Altikat, Sayit | |
| dc.contributor.author | Coban, Abdulkadir | |
| dc.contributor.author | Ciftci, Mehmet | |
| dc.contributor.author | Ozdemir, Hasan | |
| dc.date.accessioned | 2026-10-18T20:30:52.765331272Z | |
| dc.date.available | 2026-10-18T20:30:52.765331272Z | |
| dc.date.issued | 2006 | |
| dc.description.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 I 50 values of 0.414, 1.29, 1.8, 3.83, and 8.64 mM, respectively. © 2006 Taylor & Francis. | |
| dc.identifier.doi | 10.1080/14756360500483453 | |
| dc.identifier.endpage | 234 | |
| dc.identifier.issn | 1475-6374 | |
| dc.identifier.issue | 2 | |
| dc.identifier.pmid | 16789438 | |
| dc.identifier.scopus | 2-s2.0-33746139318 | |
| dc.identifier.startpage | 231 | |
| dc.identifier.uri | https://rdlopen.rawdatalibrary.net/r/ebyu/16042 | |
| dc.identifier.volume | 21 | |
| dc.language.iso | en | |
| dc.relation.ispartof | Journal of Enzyme Inhibition and Medicinal Chemistry | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.subject | Catalase | |
| dc.subject | Drug | |
| dc.subject | Human skin | |
| dc.subject | Inhibition | |
| dc.subject | Purification | |
| dc.subject | Anti-Inflammatory Agents, Non-Steroidal | |
| dc.subject | Diclofenac | |
| dc.subject | Dose-Response Relationship, Drug | |
| dc.subject | Enzyme Inhibitors | |
| dc.subject | Humans | |
| dc.subject | Inhibitory Concentration 50 | |
| dc.subject | Ketoprofen | |
| dc.subject | Piroxicam | |
| dc.subject | Skin | |
| dc.subject | Sulfamethoxazole | |
| dc.subject | ammonium sulfate | |
| dc.subject | metronidazole | |
| dc.subject | article | |
| dc.subject | concentration response | |
| dc.subject | controlled study | |
| dc.subject | drug mechanism | |
| dc.subject | enzyme analysis | |
| dc.subject | enzyme inhibition | |
| dc.subject | enzyme purification | |
| dc.subject | enzyme specificity | |
| dc.subject | human | |
| dc.subject | human tissue | |
| dc.subject | IC 50 | |
| dc.subject | in vitro study | |
| dc.subject | inhibition kinetics | |
| dc.title | In vitro effects of some drugs on catalase purified from human skin | |
| dc.type | Article | |
| dspace.entity.type | Publication | |
| rdl.citation.scopus | 13 | |
| rdl.oa.status | open | |
| rdl.source.index | SCOPUS |
