Activities of aromatic L-amino acid decarboxylase with L-dopa as substrate in brush-border- and basolateral membranes and cytoplasm obtained from rat renal cortex.
Activities of aromatic L-amino acid decarboxylase (AADC) with L-dopa as its substrate were determined in the plasma membranes and other cellular components isolated from rat renal cortex. The cytoplasm contained a high level of AADC activity, but much lower levels were found in the brush-border- and basolateral membranes. The main site involved in the formation of dopamine from L-dopa was considered to be the cytoplasm, with participation of neither the brush-border- nor the basolateral membranes.
Yamazaki
N
N
Department of Toxicology and Clinical Pharmacology, Faculty of Pharmaceutical Sciences, Higashi-Nippon-Gakuen University, Hokkaido, Japan.
Sudo
J
J
D000818:Animals; D001142:Aromatic-L-Amino-Acid Decarboxylases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D003593:Cytoplasm / Q000201:enzymology; D066298:In Vitro Techniques; D007672:Kidney Cortex / Q000201:enzymology*; D007687:Kidney Tubules, Proximal / Q000201:enzymology; D007980:Levodopa / Q000378:metabolism*; D008297:Male; D008871:Microvilli / Q000201:enzymology; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology
D007980:Levodopa; D001142:Aromatic-L-Amino-Acid Decarboxylases