Kinetic properties of the porcine kidney prolidase

Memelilerde, prolidaz tarafından katalizlenen reaksiyonun iki önemli fizyolojik fonksiyonu vardır. Birincisi prolin döngüsünün tamamlandığı kollajen degradasyonu, ikincisi ise diyet proteinlerinin sindirimindedir. Bu çalışmanın amacı; böyle önemli görevlere sahip olan bu enzimin kinetik özelliklerini domuz böbrek prolidazı kullanılarak saptanmasıdır. Bu çalışmada domuz böbrek prolidazının kinetik özellikleri, bazı metal iyonlarının ( Mn+2, Fe+2, Zn+2, Hg+2, Mg+2, Cu+2, Sr+2 ) ve bazı maddelerin etilendiamintetra asetikasid (EDTA), Iyodoasedamid (IAA), p-kloromerkuribenzoate (p-CMBA), glutatyon enzim aktivitesi üzerine etkisi incelenmiştir. Domuz böbrek prolidaz aktivitesinin Mn+2 iyonu ile 9.5 kez arttığı saptanmıştır. İncelenen diğer metal iyonları daha az aktivatör etki gösterirken Sr+2 iyonunun inhibitör etki gösterdiği tespit edilmiştir. Gly-pro substratı için Km değeri 11mmol/l, ala-pro substratı için 12mmol/l olarak saptanmıştır. Enzim aktivitesinin EDTA, İAA ve p-CMBA ile inhibe olduğu görülmüştür. Bu etkinin ise preinkübasyon ortamında daha güçlü olduğu tespit edilmiştir.
Anahtar Kelimeler:

Dipeptidazlar, Kinetik

Domuz böbrek prolidazının kinetik özellikleri

The reaction catalyzed by prolidase serves two important physiological functions in mammals. It catalyzes the final step in collagen degradation which completes the recycling of proline. A second important physiological function of prolidase is in the digestion of dietary proteins. Aim of this study, the kinetic properties was obtained of this enzyme which have such as important functions used by porcine kidney prolidase. In this study, kinetic properties of the porcine kidney prolidase, effects of some metal ions (Mn+2, Fe+2, Mn+2, Hg+2, Mg+2, Cu+2, Sr+2 ) and substances etilendiamintetraaceticacid (EDTA), Iodoacedamid (IAA), p-choloromercuri benzoate (p-CMBA), glutathione on the enzyme activity were investigated. Porcine kidney prolidase activity was increased 9,5 times with Mn+2. Other metal ions investigated caused less activator effect except for Sr+2 which had an inhibitory effect. Km values were 11mmol/l, 12 mmol/l for gly-pro and ala-pro respectively. The enzyme activity was inhibited by EDTA, IAA and p-CMBA. This effect was more effective in preincubation compared to incubation media.
Keywords:

Dipeptidases, Kinetics,

Kaynakça

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