Studies on the isolation and properties of renin granules from the rat kidney cortex.
The present study was undertaken to isolate and investigate some physicochemical properties of renin granules from the rat kidney cortex. Two preparations of subcellular organelles were used: a primary-granule fraction, which allowed the properties of lysosomes to be compared simultaneously with those of renin granules, and a semi-purified preparation of the latter. The specific activity of renin in the primary-granule preparations was about 4-fold higher than in the original homogenate; that of the semi-purified renin-granule preparation was about 18-fold higher than in the homogenate, and consisted mainly of electron-dense granules but some mitochondria were also observed. Renin and acid phosphatase release from the primary-granule preparation was increased by lowering osmolality, by a low-molecular-weight solute (glucose) and by Triton X-100 or digitonin. Enzyme release was decreased by lowering the incubation temperature (4 degrees C) or the presence of CaCl2. Renin release from the partially purified granule preparation was not affected by cyclic AMP, cyclic GMP and ATP.
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D003594:Cytoplasmic Granules / Q000187:drug effects / Q000201:enzymology / Q000648:ultrastructure; D005260:Female; D066298:In Vitro Techniques; D007672:Kidney Cortex / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D009711:Nucleotides / Q000494:pharmacology; D051381:Rats; D012083:Renin / Q000378:metabolism*; D012709:Serum Albumin / Q000494:pharmacology
D009711:Nucleotides; D012709:Serum Albumin; D000135:Acid Phosphatase; D012083:Renin