[Urinary elimination of multiple forms of gamma-glutamyltranspeptidase and aminopeptidase (author's transl)].

Concentrated and dialyzed 24-h urines of healthy persons were separated by 105000 X g ultracentrifugation into a pellet (P105) and a supernatant (S105) fraction. Chromatography of the P105 fraction on Sepharose 4B and 2B revealed that gamma-glutamyltranspeptidase and aminopeptidase activities had a molecular mass of 20 X 10(5) to 40 X 10(6), whereas in the S105 fraction soluble gamma-glutamyltranspeptidase and aminopeptidase had 86000 and 160000, respectively. Triton X-100 solubilization was performed on the P105 fraction and on a human renal cortex 40000 X g pellet, used as a reference. All the activity was recovered in both cases in a single peak of detergent gamma-glutamyltranspeptidase and detergent aminopeptidase eluted by filtration on Ultrogel Ac A22. Apparent molecular mass of Triton X-100 solubilized urinary and renal enzymes were 250000 and 243000 for gamma-glutamyltranspeptidase, and 298000 for both aminopeptidases. Protease solubilized forms were obtained by trypsic digestion of detergent urinary and renal forms. Both gamma-glutamyltranspeptidases were found to have an apparent molecular mass of 86000 on Sephadex G 150, which is identical to the value found for the S105 urinary gamma-glutamyltranspeptidase. The aminopeptidases had 238000 and 232000, which is a higher value than the molecular mass of the S105 urinary aminopeptidase. This letter could be a degraded form of the renal aminopeptidase. These findings suggest that gamma-glutamyltranspeptidase and aminopeptidase in the P105 fraction are similar to native renal enzymes. Evaluation of the P105 fraction enzymatic activities may thus be useful in the diagnosis of tubular damage.