Zobrazeno 1 - 10
of 11
pro vyhledávání: '"David G. Lygre"'
Autor:
Michael A. Walls, David G. Lygre
Publikováno v:
Canadian Journal of Biochemistry. 58:673-676
Inhibition of rat liver microsomal glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase, EC 3.1.3.9) by orthophosphate and organophosphate esters was examined at pH 6.0 and 7.5 with and without enzyme pretreatment with 0.2% (w/v) deoxycholat
Autor:
David G. Lygre
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 341:291-297
Saccharin and cyclamate were found to inhibit the glucose-6-phosphate phosphohydrolase and PPi-glucose phosphotransferase activities of beef liver microsomal glucose-6-phosphatase (d-glucose-6-phosphate phosphohydrolase, EC 3.1.3.9). The extent of in
Autor:
David G. Lygre
Publikováno v:
Canadian Journal of Biochemistry. 54:587-590
Inhibition by saccharin of rat liver glucose-6-phosphatase (EC 3.1.3.9) generally decreased as the pH increased in the range pH 4–8. This pattern was exhibited by homogenates from control and alloxan-treated animals assayed each in the absence and
Autor:
Robert C. Nordlie, David G. Lygre
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 185:360-366
The inhibition by phlorizin of rabbit intestinal d -glucose-6-phosphate phosphohydrolase (EC 3.1.3.9) and of PPi-glucose phosphotransferase activity also catalyzed by this enzyme was investigated. studies were carried out with freshly prepared, unsup
Autor:
Robert C. Nordlie, David G. Lygre, James F. Soodsma, T.L. Hanson, William J. Arion, Richard N. Horne, Wayne B. Anderson, J R Gilsdorf
Publikováno v:
Journal of Biological Chemistry. 243:1140-1146
The effects of fasting on hydrolytic and synthetic activities of liver microsomal glucose 6-phosphate phosphohydrolase (EC 3.1.3.9) have been investigated. Differential responses of the two types of activity were observed. Glucose 6-phosphate and ino
Autor:
David G. Lygre, Robert C. Nordlie
Publikováno v:
Journal of Biological Chemistry. 241:3136-3141
Rat liver microsomal glucose 6-phosphatase previously has been shown to catalyze an inorganic pyrophosphate-glucose phosphotransferase reaction. Citrate, which has been employed as a buffer in some earlier studies of this enzyme, recently has been fo
Publikováno v:
Proceedings of the National Academy of Sciences. 60:590-597
Publikováno v:
Journal of Biological Chemistry. 247:6299-6305
Transcarboxylase labeled with 60Co or 65Zn was isolated and purified to near homogeneity from Propionibacterium shermanii. The enzyme which is a metallo-biotin enzyme, was found to contain 7 to 8 g atoms of zinc plus cobalt per mole of transcarboxyla
Autor:
David G. Lygre, Edward P. Lau
Publikováno v:
Biochimica et biophysica acta. 309(2)
A soluble fraction from cotyledon tissue of black mustard (Brassica nigra) was found to catalyze the hydrolysis of glucose 6-phosphate. In an attempt to determine whether this reaction was catalyzed by a distinct glucose-6-phosphate (d-glucose 6-phos
Autor:
David G. Lygre, Robert C. Nordlie
Publikováno v:
Biochemistry. 7(9)