We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin'in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri.
- Authors
ÖZYÜREK, Işıl Nihan; KALIN, Ramazan; ÖZDEMİR, Hasan
- Abstract
The lactoperoxidase (LPO, E.C.1.11.1.7) secreted from the breast, saliva and other mucous glands is a peroxidase enzyme with antibacterial properties. D-penicillamine is an amino acid with a thiol side chain, used in the treatment of many diseases such as Wilson disease. The aim of this study was to determine in vitro inhibition profiles of D-Penicillamine, D-Penicillamine disulfide and N-Acetyl-D-penicillamine against bovine lactoperoxidase enzyme. LPO enzyme was isolated from bovine milk using affinity chromatography (Sepharose 4B-L-tyrosine-sulphanamide) 357.92 fold with a yield of 62.25%. LPO was effectively inhibited by D-Penicillamine, N-Acetyl-D-penicillamine and D-Penicillamine disülfit. IC50 values of these molecules were found as 0.584, 0.207 and 0.552 µM, respectively. D-Penicillamine, and D-Penicillamine disülfit exhibited competitive inhibition, and N-Acetyl-D-penicillamine showed noncompetitive inhibition.
- Subjects
AFFINITY chromatography; SEPHAROSE; AMINO acids; LACTOPEROXIDASE; ENZYMES
- Publication
Journal of the Institute of Science & Technology / Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi, 2020, Vol 10, Issue 2, p1146
- ISSN
2146-0574
- Publication type
Article
- DOI
10.21597/jist.669441