Characterization of ATPase activity in the mycelial form cells of yeast Saccharomycopsis fibuligera.
1. The properties of ATPase activity were studied with the mycelial form cells of Saccharomycopsis fibuligera. 2. Optimal pH for the activity was about 9.5. 3. The activity was stimulated by Mg2+. 4. The activity was inhibited by DCCD, NaF and oligomycin, but not inhibited by ouabain.
Ota
A
A
Medical School, Osaka University, Japan.
Morishita
H
H
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D009840:Oligomycins / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D004718:Saccharomycetales / Q000201:enzymology*; D012442:Saccharomycopsis / Q000166:cytology / Q000201:enzymology* / Q000254:growth & development; D012969:Sodium Fluoride / Q000494:pharmacology
D009840:Oligomycins; D004024:Dicyclohexylcarbodiimide; D010042:Ouabain; D000255:Adenosine Triphosphate; D012969:Sodium Fluoride; D000251:Adenosine Triphosphatases; D008274:Magnesium