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. 1978 May 15;172(2):233–238. doi: 10.1042/bj1720233

An energy requirement for the degradation of intravenously injected 125I-labeled albumin in mouse liver and kidney slices.

J L Mego, R M Farb
PMCID: PMC1185688  PMID: 666741

Abstract

Liver and kidney slices prepared 30min after intravenous injections of formaldehyde-treated 125I-labelled bovine serum albumin into mice degrade approx. 25-40% of the protein to a trichloroacetic acid-soluble form during 60min incubation at 37 degrees C. The presence of bicarbonate in Krebs-Ringer phosphate medium inhibited intracellular proteolysis, and similar results were obtained at pH5 or pH7 in kidney or liver slices. Cellular integrity was required to obtain substantial rates of proteolysis. This intralysosomal intracellular degradation of an exogenous protein was partially inhibited by inhibitors of oxidative ATP formation, such as cyanide, azide, 2,4-dinitrophenol and absence of oxygen. Arsenite and iodoacetamide were also effective inhibitors, but the effects of fluoride were variable. These results suggest that an energy requirement exists for intralysosomal proteolysis in intact cells and are consistent with the hypothesis that energy may be required to maintain intralysosomal acidity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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