Özet:

Lactoperoxidase (LPO, E.C.1.11.1.7) is a peroxidase enzyme with antibacterial properties. D-Penisylamine is an amino acid with the tiol side chain used in the treatment of many diseases such as Wilson's disease. The aim of this study is to determine the in vitro inhibition profiles of D-Penisylamine, D-Penisylamine disulfite and N-Asetyl-D-Penisylamine against cattle lactoperoxidase enzyme. The LPO enzyme was purified from livestock milk using 357.92 times affinity chromatography (Sepharose 4B-L-thyrozin-sulfanamide) with a 62.25% efficiency. LPO was effectively inhibited by D-Penisylamine, D-Penisylamine disulfite and N-Asetyl-D-Penisylamine. The IC50 values of these molecules were found at 0,584, 0,207 and 0,552 μM respectively. While D-Penisylamine and D-Penisylamine showed competitive inhibition for dysulfite, N-Asetyl-D-Penisylamine showed competitive inhibition.

Anahtar Kelimeler:

Özet:

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.