The locations of cathepsin activity and β-glucuronidase in the Guerin T8 tumour
Keyword(s):
Tumour homogenate fractions, isolated by differential centrifugation, were subfractionated by density-gradient centrifugation. Biochemical and electron microscopic analyses revealed that β-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 0.2μm in diameter. β-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.
2017 ◽
pp. 113-131
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1970 ◽
Vol 23
(5)
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pp. 1197
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1966 ◽
Vol 30
(2)
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pp. 405-415
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