The locations of cathepsin activity and beta-glucuronidase in the Guerin T8 tumour.
Tumour homogenate fractions, isolated by differential centrifugation, were subfractionated by density-gradient centrifugation. Biochemical and electron microscopic analyses revealed that beta-glucuronidase and cathepsin activity were associated with a class (possibly two) of lysosomal particles of density greater than those of mitochondria and the endoplasmic reticulum. Lysosomes sedimented by low g forces were vacuolar, electron-dense, delineated by a unit membrane and about 0.2mum in diameter. beta-Glucuronidase was also apparently associated with ribosomes whereas cathepsin was bound in part to the endoplasmic reticulum. Catalase and glucose 6-phosphatase possessed slightly different density-gradient sedimentation profiles.
D000818:Animals; D002374:Catalase / Q000032:analysis; D002403:Cathepsins / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D004721:Endoplasmic Reticulum / Q000201:enzymology; D005260:Female; D005952:Glucose-6-Phosphatase / Q000032:analysis; D005966:Glucuronidase / Q000032:analysis*; D008247:Lysosomes / Q000201:enzymology; D008854:Microscopy, Electron; D009374:Neoplasms, Experimental / Q000201:enzymology*; D051381:Rats
D002374:Catalase; D005952:Glucose-6-Phosphatase; D005966:Glucuronidase; D002403:Cathepsins