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Electrophoretic variants of alanine amino peptidase ec 3.4.11.2 alkaline phosphatase ec 3.1.3.1 and gamma glutamyl transferase ec 2.3.2.2 in urine


, : Electrophoretic variants of alanine amino peptidase ec 3.4.11.2 alkaline phosphatase ec 3.1.3.1 and gamma glutamyl transferase ec 2.3.2.2 in urine. Clinical Chemistry 30(6): 856-859

The 3 brush-border enzymes, alanine aminopeptidase, alkaline phosphatase and .gamma.-glutamyltransferase, are present in the urine of healthy persons in 2 variants, a particulate form and a soluble one. They can be separated by electrophoresis in agarose gel and by ultracentrifugation. The particulate forms exhibit similar electrophoretic mobility, but the soluble forms of these brush-border enzymes differ in their electrophoretic mobilities. The enzyme components of the particulate activity can be mobilized by Triton X-100 and trypsin. The electrophoretic mobility of the soluble forms of alanine aminopeptidase and .gamma.-glutamyltransferase is slowed by neuraminidase treatment. Both forms of .gamma.-glutamyltransferase are influenced in their electrophoretic mobility by treatment with n-butanol/diisopropyl ether, showing their lipid dependence. These findings enhance knowledge of the biochemical nature of brush-border enzymes in urine.

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