[Purification and properties of acid alpha-glucosidase (gamma-amylase) from the human liver].
Acid alpha-glucosidase from human liver was 720-fold purified by means of a specific sorption on Sephadex G-150 and a specific desorption from Sephadex by the competitive inhibitor, methyl-alpha-D-glucopyranoside. The preparation obtained was homogenous in ultracentrifuge and polyacrilamide gel electrophoresis. The enzyme possessed both maltase and glucoamylase activities and splitted maltose, amylopectin and glycogen with Km values of 7mM, 7.7 mg/ml and 5 mg/ml respectively. Methyl-alpha-D-glucopyranoside competitively inhibited the enzymatic hydrolysis of polysaccharides (Ki=6.95 mM) and did not affect the maltose degradation. The sedimentation coefficient of the purified enzyme preparation was 5.4 S; in 5 M guanidine. HCl the coefficient decreased to 2.2 S, which testified to the fact that the enzyme molecule consisted of subunits.
D000687:Amylopectin / Q000378:metabolism; D002850:Chromatography, Gel; D005959:Glucosidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D006003:Glycogen / Q000378:metabolism; D006146:Guanidines; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008320:Maltose / Q000378:metabolism; D008757:Methylglucosides / Q000494:pharmacology; D011134:Polysaccharides / Q000378:metabolism; D014461:Ultracentrifugation
D006146:Guanidines; D008757:Methylglucosides; D011134:Polysaccharides; D008320:Maltose; D006003:Glycogen; D000687:Amylopectin; D005959:Glucosidases
Ochistka i svoistva kisloĭ al'fa-gliukozidazy (gamma-amilazy) iz pecheni cheloveka