Influence of Certain Amino Acids Upon the Enzymic Hydrolysis of Starch

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Further experiments were performed in which the cupric sulphate was added directly to the enzyme solution in two concentrations, 0. 0035 M and 0. 00003 M and the efficiency of 0. 1 per cent glycine in the substrate in reactivating the enzyme was studied. Some results are given in Table VII. 10 Jour. Amer. Chem. Soc. , 43, 2454 (1921). Upon the Enzymic Hydrolysis of Starch 11 TABLE VII Reactivation of Pancreatic Amylase by Glycine after Inactivation by Copper _ o . S . Sg -ss QV o*3 O-g i CAM Wo... R fl s g. M, =? c Cuprous oxide J5> " S - 2 5 O "5 E O gJ3 g| 8 Exp. L Exp. 2 Exp. 3 Mg. Uto U U-5 Mg. Mg. Mg. 00 280 252 264 100 316 300 100 0. 0035 M 0. 00003 M 98 0. 0035 M 0. 00003 M 4 0. 00003 M 0. 00000018 M 209 100 0. 00003 M 0. 00000018 M 260 184 100 0. 00003 M 0. 00003 M 0. 00003 M 260 182 Numerous experiments showed that the inactivation of the enzyme by the copper and its reactivation by amino acid were considerably influenced by time and temperature. In Expt. 2 of Table VII the solution stood for 12 minutes before testing; in Expt.

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