[Acid gamma-amylase of rabbit and human brain].
Preparations of acidic gamma-amylase, which cleaved glycogen and maltose, were isolated from human and rabbit brain tissues. The specific activity of the gamma-amylase preparations from human brain was approximately twice higher than the activity of the enzyme from rabbit brain. In degradation of glycogen gamma-amylases from human and rabbit brain had the pH optima at pH 4.9 and 4.6 and with maltose as a substrate- at pH 4.3 and 4.1, respectively. gamma-Amylases from both sources possessed the high stability in presence of monovalent cations. K+ distinctly increased the cleavage of glycogen by gamma-amylase from human and rabbit brain. alpha, alpha-Trehalose and alpha-menthyl glucoside proved to be inhibitors of the glucoamylase activity of the enzymes from both sources. Km values of the gamma-amylases for glycogen were equal to 19.3 mM 19.8 and for maltose -5.54 mM and 5.78 mM, respectively. The data obtained suggest that acidic gamma-amylases from human and rabbit brain are similar to acidic gamma-amylases from other sources.
D000681:Amylases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D006003:Glycogen; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008320:Maltose; D008757:Methylglucosides / Q000494:pharmacology; D011817:Rabbits; D013696:Temperature; D014199:Trehalose / Q000494:pharmacology
D008757:Methylglucosides; D008320:Maltose; D006003:Glycogen; D014199:Trehalose; D000681:Amylases
Kislaia gamma-amilaza mozga cheloveka i krolika