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- W2057751565 abstract "1. Lysosome-rich fraction (M+L) were sub-fractionated by S-ϱ zonal separations in sucrose gradients containing 0.02 M KCl. THe fractions were assayed for proteins, cytochrome oxidase, 3 acid hydrolases (cathepsin D, p-nitrophenolphosphatse, and β-glucuronidase), catalase, and 2 ATPases (Ca2+-activated and EGTA-ATPase). 2. Two major fractions were isolated that had different S-ϱ coordinates. These two fractions contained enzyme markers for: lysosomes; SR fragments, some of which may possess acid hydrolase activity; mitochondria; and catalase containing vesicles. 3. Incubation of the two fractions with Ca2+ and ATP shifted lysosomes and a portion of the sarcoplasmic reticulum to a denser part of the sucrose gradient. 4. EDTA (lmM) in the homogenizing media caused an alteration in the equilibrium density of lysosomes and a portion of the sarcoplasmic reticulum. 5. The EDTA alteration could be partially reversed by the addition of Ca2+ and ATP." @default.
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- W2057751565 date "1974-01-25" @default.
- W2057751565 modified "2023-09-23" @default.
- W2057751565 title "S-ϱ zonal fractionation studies of rat skeletal muscle lysosome-rich fractions☆" @default.
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- W2057751565 doi "https://doi.org/10.1016/0304-4165(74)90352-3" @default.
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