Subcellular fractions were prepared from mouse kidney homogenates by differential and sucrose-gradient centrifugation. A fraction enriched in Golgi apparatus was obtained, which had considerably enriched galactosyltransferase and thiamin pyrophosphatase activities, and was morphologically typical of Golgi material. This preparation also had high β-glucuronidase activity, which increased concomitantly with microsomal β-glucuronidase activity during the specific stimulation of the enzyme in male mouse kidney after androgen administration. The degree of stimulation was much greater in the Golgi fraction. Gel-electrophoretic patterns of Golgi β-glucuronidase resembled more closely those of the enzyme located within lysosomes, but contained minor bands similar to those described previously (Swank & Paigen, 1973) as characteristic of the microsomal enzyme. It was concluded that the Golgi complex is involved in the distribution of the enzyme after its synthesis to both lysosomal and microsomal fractions.
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Research Article|
September 01 1974
Golgi β-glucuronidase of androgen-stimulated mouse kidney
Charles A. Marsh;
Charles A. Marsh
1Tufts Cancer Research Center and the Department of Pathology (Oncology), Tufts University School of Medicine, Boston, Mass. 02111, U.S.A.
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Chi-Wei Lin;
Chi-Wei Lin
1Tufts Cancer Research Center and the Department of Pathology (Oncology), Tufts University School of Medicine, Boston, Mass. 02111, U.S.A.
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William H. Fishman
William H. Fishman
1Tufts Cancer Research Center and the Department of Pathology (Oncology), Tufts University School of Medicine, Boston, Mass. 02111, U.S.A.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1974 London: The Biochemical Society
1974
Biochem J (1974) 142 (3): 491–497.
Citation
Charles A. Marsh, Chi-Wei Lin, William H. Fishman; Golgi β-glucuronidase of androgen-stimulated mouse kidney. Biochem J 1 September 1974; 142 (3): 491–497. doi: https://doi.org/10.1042/bj1420491
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