AI Summary & Key Takeaways
AI InsightBoth peroxides inhibited the enzyme activity, however their effects were different and t-BHP has more inhibitory effect than H2Ö2-
📌 3 Key Takeaways
Abstract
Activity of human erythrocyte membrane Ca^+ ATPase which is responsible for maintaining the inside and outside Ca concent¬ration of the cell within physiological limits, was measured by using different incubation mediums. The effect of calmodulin (CaM) on the activity of the enzyme was investigated. Maximum velocity of the reaction (specific activity) (Vm), Michaelis-Menten Coefficient (Km) and activation energy (Ea) were determined as 16 [xmol Pilmg prot.h, 1.9 mM and 4.5 kcallmol, respectively. Effects of two activated oxygen species, tert-butyl hydroperoxide (t-BHP) and hydrogen peroxide (H2O2) on the enzyme activity were also determined. Both peroxides inhibited the enzyme activity, however their effects were different and t-BHP has more inhibitory effect than H2Ö2-
Özet
Hayvansal organizmaların hücre içi ve hücre dışı kalsiyum- iyonlarının fizyolojik sınırlar içerisinde sabit tutulmasından sorumlu olan Ccr+ ATPaz enziminin aktivitesi insan eritrosit zarlarında farklı inkübasyon ortamları kullanılarak ölçülmüş, enzimin aktivatörü olduğu bildirilen kalmodulinin (CaM) enzim aktiyitesine etkisi incelenmiştir. Enzimatik reaksiyonun maksimum hızı (Vm), 16 fimol Pilmg prot. saat, Michaelis Menten hız sabiti (Km), 1,9 mM ve aktivasyon enerjisi (Ea), 4,5 kkal/mol olarak bulunmuştur. Aktif oksijen bileşiklerinden hidrojen peroksit (H2O2) ve tersiyer butil hidroperoksitin (t-BHP) enzim aktivitesini azalttığı ancak t-BHP'in H2Û2'ye göre daha fazla inhibisyon etkisine sahip olduğu saptanmıştır.