Properties of the alpha-glucosidase from various human tissues in relation to glycogenosis type II (Pompe's disease).
The physico-chemical and electrophoretical properties of alpha-glucosidases from various human tissues and urine have been studied. There were some differences among Peak I enzymes (neutral alpha-glucosidases) obtained from liver, heart, muscle, kidney and urine. These differences are based on different effects of tris(hydroxymethyl)aminomethane and various thermostabilities of the Peak I enzymes. Electrophoretically, the Peak I enzyme activity at pH 6.5 from control tissues displayed a two-banded pattern except in kidney and urine. In the patient with the adult form of Pompe's disease the faster band of the Peak I enzyme from heart and muscle was not found and the slower band of the Peak I enzyme from liver was more cathodic. The results are discussed in relation to glycogenosis type II (Pompe's disease).
D003300:Copper / Q000494:pharmacology; D004586:Electrophoresis; D005959:Glucosidases / Q000378:metabolism*; D006008:Glycogen Storage Disease / Q000201:enzymology*; D006009:Glycogen Storage Disease Type II / Q000201:enzymology*; D006358:Hot Temperature; D006801:Humans; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D011189:Potassium Chloride / Q000494:pharmacology; D014325:Tromethamine / Q000494:pharmacology
D014325:Tromethamine; D011189:Potassium Chloride; D003300:Copper; D005959:Glucosidases