Electrophoretic variants of alanine aminopeptidase, alkaline phosphatase, and gamma-glutamyltransferase in urine.
The three brush-border enzymes--alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), and gamma-glutamyltransferase (EC 2.3.2.2)--are present in the urine of healthy persons in two 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 our knowledge of the biochemical nature of brush-border enzymes in urine.
D000469:Alkaline Phosphatase / Q000652:urine*; D000626:Aminopeptidases / Q000652:urine*; D018826:CD13 Antigens; D004587:Electrophoresis, Agar Gel; D006801:Humans; D007527:Isoenzymes / Q000652:urine; D007668:Kidney / Q000201:enzymology; D008871:Microvilli / Q000201:enzymology; D009439:Neuraminidase / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D014461:Ultracentrifugation; D005723:gamma-Glutamyltransferase / Q000652:urine*
D007527:Isoenzymes; D005723:gamma-Glutamyltransferase; D000469:Alkaline Phosphatase; D009439:Neuraminidase; D000626:Aminopeptidases; D018826:CD13 Antigens; D014357:Trypsin