Kinetic properties of potassium stimulated ATPase purified from gastric mucosa.
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.
Tükel
S
S
University of Cukurova, Medical Faculty, Department of Biochemistry, Balcali, Adana, Turkey.
Isbir
T
T
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004795:Enzyme Stability; D005753:Gastric Mucosa / Q000201:enzymology*; D017506:H(+)-K(+)-Exchanging ATPase; D007700:Kinetics; D010295:Parietal Cells, Gastric / Q000201:enzymology; D011898:Ranidae; D013816:Thermodynamics
D000251:Adenosine Triphosphatases; D017506:H(+)-K(+)-Exchanging ATPase