TY - JOUR
T1 - Detection of an atpase activity in rat liver peroxisomes
AU - del Valle, Ruth
AU - Soto, Ubaldo
AU - Necochea, Cecilia
AU - Leighton, Federico
N1 - Funding Information:
Acknowledgements: This work was supported by the Fondo Nacional de Ciencia y Tecnologla, project 627-87 and the Direccidn de Investigacidn, Universidad Catdlica de Chile, project 79-86.
PY - 1988/11/15
Y1 - 1988/11/15
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/0023736173
UR - https://www.scopus.com/pages/publications/0023736173#tab=citedBy
U2 - 10.1016/S0006-291X(88)80781-2
DO - 10.1016/S0006-291X(88)80781-2
M3 - Article
C2 - 2973319
SN - 0006-291X
VL - 156
SP - 1353
EP - 1359
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -