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

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In: Weber G (ed) Advances in enzyme regulation, vol XI. Pergamon Press, Oxford, p 169-191 23. Millward DJ, Garlick PJ (1974-1976) Protein turnover and cellular environment. In: Hanson H, Bohley P (eds) Intracellular protein catabolism. Barth, Leipzig, p 158-164 24. Bohley P, Kirschke H, Langner J, Wiederanders B, Ansorge S, Hanson H (1974-1976). Degradation of rat liver proteins. In: Hanson H, Bohley P (eds) Intracellular protein catabolism. Barth, Leipzig, p 201-209 25. Bohley P, Kirschke H, Langner J, Ansorge S (1969) Praparative Gewinnung hochgereinigter Lysosomenenzyme aus Rattenlebern.

However, direct evidence for this conclusion is still lacking. Progress in elucidating the actual role played by the nucleoside triphosphates has been slow indeed and the source of appreciable frustration. One major technical problem has been that the stimulation by ATP is very labile. In addition, these preparations do contain appreciable ATPase activity. Consequently, it has also been impossible thus far to determine whether the high energy phosphate bond is actually cleaved during the proteolytic process.

The products of this ATP-dependent activity were large acid-soluble peptides. By contrast, the end-products of proteolysis in the crude E. coli extracts are free amino acids. Thus the complete degradation of protein appears to involve the concerted actions of an ATP-dependent endoprotease and a number of other proteases and peptidases (see below). By an elegant mutant analysis, Charles Miller and colleagues (Miller, 1979) have clearly demonstrated a role for various peptidases in the final steps of the degradative process.

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