CHANGES IN THE ACTIVITY OF ACID HYDROLASES DURING RENAL REABSORPTION OF LYSOZYME

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Abstract
Present studies quantitatively describe the cycle of injected lysozyme and the concomitant changes in the specific activity of acid hydrolases in mouse kidney cortex. The increase in acid ribonuclease activity corresponds to the phase of lysozyme accumulation and that of cathepsin activity to the leveling off and disappearance of the protein from renal cortex. It was demonstrated that actinomycin D inhibits the increase in acid ribonuclease but has no effect on the increase in cathepsin. The results suggest that the increase in acid ribonuclease is due to a de novo synthesis of the enzyme and it is possible that the changes in cathepsin activity are a result of the stabilization of the enzyme by its substrate. The relationship between renal uptake of proteins and the role of acid hydrolases and lysosomes is briefly discussed.