Kinetic properties of potassium stimulated ATPase purified from gastric mucosa.
نویسندگان
چکیده
In this study, partially purified K+-H+ ATPase from frog gastric mucosa were obtained by using differential and density gradient centrifugation. Optimum activity of K+-H+ ATPase (Vmax), Michealis-Menten constant (Km) and Hill coefficient (h) were found as 83.3 mumol Pi.mg prot-1.h-1, 95.2 microM and 0.91, respectively. Enzyme preparations were more stable in glycerol solutions stored at -40 degrees C. Minimum activity lost was determined for samples stored in 40% (v/v) glycerol solution at -40 degrees C for two months.
منابع مشابه
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عنوان ژورنال:
- Zeitschrift fur Naturforschung. C, Journal of biosciences
دوره 43 7-8 شماره
صفحات -
تاریخ انتشار 1988