[Two forms of alkaline phosphatase in blood serum in liver diseases].
A fraction whose electrophoretic mobility in polyacrylamide gel corresponded to the liver isoenzyme was produced due to trypsin hydrolysis of the high-molecular alkaline phosphatase of blood serum of patients suffering from liver diseases and of liver homogenates. In the presence of positively and negatively charged micelles of detergents the electrophoretical mobility of high-molecular alkaline phosphatase in agarose changed essentially as compared to that in the presence of the noncharged detergent micelles. Similar changes in mobility were not observed for the liver isoenzyme. Due to the autolysis of liver homogenates the activity of the zone corresponding to the liver isoenzyme in the electrophoretic mobility increases and that of high-molecular alkaline phosphatase decreases. Similar changes were observed in sera as well, however, their rate is lower.
D000469:Alkaline Phosphatase / Q000097:blood*; D006505:Hepatitis / Q000201:enzymology; D006801:Humans; D007527:Isoenzymes / Q000097:blood*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008107:Liver Diseases / Q000201:enzymology*; D008823:Micelles
D007527:Isoenzymes; D008823:Micelles; D000469:Alkaline Phosphatase
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