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By R. Huber (auth.), Prof. Dr. Helmut Holzer, Prof. Dr. Harald Tschesche (eds.)

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V. Bevorzugter Abbau kurzlebiger Zytosolproteine durch Lysosomenendopeptidasen aus Rattenleber. Acta Bioi Med Germ 28: 323-330 65. Katunuma N, Sanada Y, Koninami E, Kobayashi K, Banno Y (1977) Intracellular protein catabolism and new serine proteases. Acta Bioi Med Germ 36:1537-1546 66. Bohley PH, Kirschke H, Langner J, Wiederanders B, Ansorge S, Hanson H (1974) Primary reactions of intracellular protein breakdown. 9th FEBS Meet Budapest Abstr p 90 67. Segal HI, Winkler JR, Miyagi MP (1974) Relationship between degradation rates of proteins in vivo and their susceptibility to lysosomal proteases.

Touster 0 (1978) The chemistry and turnover of lysosomal enzymes. In: Segal HL, Doyle DJ (eds) Protein turnover and lysosome function. Academic Press, London New York, p 231-250 10. Dean RT, Barrett AJ (1976) Lysosomes. Essays Biochem 12:1-40 11. Goldberg AL, StJohn AC (1976) Intracellular protein degradation in mammalian and bacterial cells, Part 2. Annual Rev Biochem 45:747-803 12. Schimke RT (1964) The importance of both synthesis and degradation in the control of arginase in rat liver. J BioI Chem 239:3808-3817 13.

Coli extracts, the ATP-analogs, a-S-methylene ATP and S-y-methylene ATP did not stimulate protein degradation. In addition, arsenate, an inhibitor of many ATP-hydrolyzing enzymes, decreased proteolysis in the presence of ATP, but not in its absence (Voellmy and Goldberg, 1978). These observations are consistent with hydrolysis of ATP by the degradative system. Evidence for a Membrane-Association of the ATP-Stimulated Activity Initially we had assumed that this proteolytic activity was derived from the soluble fraction of the cell, since the activity was recovered in the supernatant upon centrifugation at 30,000 g.

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