Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and Percoll gradients.
Crude chromaffin secretory vesicles, obtained by differential centrifugation, were further purified on isotonic (Percoll) gradients. The chromaffin vesicle fractions recovered from the gradients contain acetylcholinesterase as well as lysosomal enzymes. With the aid of a subsequent sucrose gradient lysosomal enzymes could be removed from chromaffin vesicle fractions, but not acetylcholinesterase. This suggests that lysosomal enzymes do not pass through the chromaffin vesicles during the biogenesis of lysosomes but acetylcholinesterase does.
D000110:Acetylcholinesterase / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D002458:Cell Fractionation / Q000379:methods; D002499:Centrifugation, Density Gradient / Q000379:methods; D002837:Chromaffin Granules / Q000201:enzymology* / Q000648:ultrastructure; D002838:Chromaffin System / Q000201:enzymology*; D006867:Hydrolases / Q000302:isolation & purification*; D008247:Lysosomes / Q000201:enzymology*; D011205:Povidone; D011506:Proteins / Q000302:isolation & purification; D012822:Silicon Dioxide; D013395:Sucrose
D011506:Proteins; D013395:Sucrose; C016039:Percoll; D012822:Silicon Dioxide; D006867:Hydrolases; D000110:Acetylcholinesterase; D011205:Povidone