Detection of an ATPase activity in rat liver peroxisomes.
An ATPase co-sedimenting with rat liver peroxisomes has been detected after subcellular fractionation. The activity is Mg2+ dependent, with pH optimum of 7.5 and is inhibited by NEM and DCCD but not by oligomycin. Partial inhibition of the mitochondrial ATPase allows to detect the peroxisomal activity in the gradients. Protease inactivation and solubilization data suggests that the activity resides in a protein of the peroxisomal membrane, exposed to the cytosol.
del Valle
R
R
Departamento de Biología Celular, Universidad Católica de Chile, Santiago.
Soto
U
U
Necochea
C
C
Leighton
F
F
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000818:Animals; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D005033:Ethylmaleimide / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008297:Male; D008830:Microbodies / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases; D005033:Ethylmaleimide