Feb 28, 1985

Characterization of proteolytic systems in human and rat urine

Biochemical and Biophysical Research Communications
U Wormser, G Zbinden

Abstract

Activities of proteolytic enzymes were detected in rat and human urine by using [125 l] iodo-insulin B chain as a substrate. The pH optimum of human urine activity was in the acidic range (pH 2.0) whereas the rat urine had two pH optima, one at the acidic range similar to human urine and another at pH 7.5. The activities were linear with time and amount of enzyme. Study with various proteinase inhibitors revealed that the acidic pH activities of human and rat urine were apparently of carboxyl endopeptidases since they were totally inhibited by pepstatin 10-8M. The neutral pH proteolysis of rat urine was inhibited by chelating agents and therefore it was considered as a metalloendopeptidase activity. These findings show the difference between the content of urinary proteolytic enzymes in humans and in rats by using a sensitive and simple radioactive assay.

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Mentioned in this Paper

A14-monoiodoinsulin
Peptide Hydrolases
Streptomyces pepsin inhibitor
Pepstatins
Edetic Acid, Sodium Salt
Insulin B Chain
Novolin
Egtazic Acid Sodium Salt
Egtazic Acid Potassium Salt
Hydrogen-Ion Concentration

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