Nonlysosomal granules in peritoneal macrophages: Subcellular localization of neutral .ALPHA.-glucosidase.

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  • SUBCELLULAR LOCALIZATION OF NEUTRAL α-GLUCOSIDASE

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Neutral α-glucosidase in mouse peritoneal macrophages was shown to be associated with granules distinct from lysosomes. When post-nuclear supernatants were centrifuged in a Percoll density gradient containing 20units/ml of heparin and 10mM Tris-HCl (pH 7.2), neutral α-glucosidase activity was clearly separated from β-glucuronidase activity. Activity peaks for alkaline phosphodiesterase, a plasma membrane enzyme, and for UDP-galactosyl transferase activity, a Golgi enzyme, were detected in different fractions. Release of the enzyme activities into extracellular medium depending on phagocytosis or pharmacological stimuli, was also different. These observations suggested that neutral α-glucosidase localize in nonlysosomal granules in macrophages.

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