By Bernard L. Horecker, Earl R. Stadtman
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Bacteriol. 91, 428-435 (1966). 67. Suhadolnik, R. " Wiley, New York, 1970. 68. Talens, L. , and Miller, M. , J. Bacteriol. 114, 413-423 (1973). 68a. , / . Biol. , in press. 69. , Arch. Mikrobiol. 70, 89-103 (1970). 70. , Eur. J. Biochem. 32, 129-135 (1973). Metabolie Regulation by Multifunctional Glucose-6-phosphatase ROBERT C. NORDLIE Department of Biochemistry University of North Dakota of Medicine Grand Forks, North Dakota I. Introduction I I . Multifunctionality and Other Characteristics of the Enzyme .
On the other hand, the inhibitor from S. cerevisiae is more negatively charged than that from S. carlsbergensis as concluded from its greater mobility in acrylamide gel electrophoresis and from its capacity to bind to DEAE-cellulose. Either inhibitor is active against the activating factor of the other species. As shown by the titration experiment of Fig. 11 the inhibitor appears to bind stoichiometrically to the activating factor. It is not known if the complex can be dissociated. There is but little information about the variations in the physiological level of inhibitor in the cell.
As shown in Table II, about 40% of the activating factor was recovered in the vacuole fraction, which contained only negligible amounts of zymogen. A 25-fold purification of activating factor with respect to protein was achieved. Most of the zymogen, free from activating factor, was found in the pellet after centrifugation (14)- These experiments confirm that zymogen and activating factor reside in different organelles, since the method used for their separation was very mild and did not include sonic oscillation.
Current topics in cellular regulation Vol. 8 by Bernard L. Horecker, Earl R. Stadtman