Chemical activity of the glucose adduct of 3‐amiuo‐ l,2,4 triazole

Gentile, Arthur C.; Frfedrick, Jerome F.

doi:10.1111/j.1399-3054.1959.tb08920.x

Cited by 17 publications

(6 citation statements)

References 3 publications

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“…This compound was prepared as described by Frederick and Gentile (12). GAT glucose in 10 ml of 60 mm sodium acetate (15). The mixture was held at 50 to 60 C for 30 hr.…”

Section: Methodsmentioning

confidence: 99%

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Purification of myo-Inositol 1-Phosphate Synthase from Rice Cell Culture by Affinity Chromatography

Funkhouser¹,

Loewus²

1975

Plant Physiol.

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myo-Inositol 1-phosphate synthase (EC 5.5.1.4) is the enzyme which catalyzes the synthesis of the precursor for the myo-inositol oxidation pathway. Rice callus grown in suspension culture provides a good source of plant enzyme. Use has been made of a noncompetitive inhibitor to prepare an affinity column for this enzyme. With this column, the enzyme from rice callus has been purified 1500-fold in a single step, about 9000-fold over-all, to a specific activity of 0.078 units per milligram of protein. This is an order of magnitude greater than previous purifications of the plant enzyme.MI4 is an intermediate in one of the two pathways by which the carbon skeletons of cell wall uronic acids and pentoses are derived from D-glucose (21). MI 1-phosphate synthase5 (EC 5.5.1.4) catalyzes conversion of glucose to MI via their phosphorylated intermediates. In plants, it provides the immediate precursor of the MI oxidation pathway (22)(23)(24). If this enzyme can be purified to homogeneity, then significant experiments involving enzymatic regulation and control of the endogenous pool of MI can be designed.Synthase activity has been observed in all plant material examined so far (16,17,19,25,29,35). It has also been found in fungi (32), yeast (5), rat testes (9), bovine testes (36), chicken erythrocytes (35), rat mammary gland (3, 4, 31) and rat liver and plasma (3). Enzyme from plant sources studied in this laboratory offers a distinct advantage over the others in that it is extremely stable. No loss of activity was noted after 1 week at 4 C or 8 months at -20 C (28).In previous attempts to purify the synthase from Acer pseudoplatanus, ammonium sulfate fractionation and chromatography on DEAE cellulose and Sephadex G-200 columns were used (25). This gave 500-to 1000-fold purification. At least seven electrophoretically distinct protein bands remained in the final preparation. At this point, insufficient material was available for

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“…This compound was prepared as described by Frederick and Gentile (12). GAT glucose in 10 ml of 60 mm sodium acetate (15). The mixture was held at 50 to 60 C for 30 hr.…”

Section: Methodsmentioning

confidence: 99%

“…After incubation at 30 C for 3 hr, the reaction was terminated by heat in a boiling water bath. The final product, P-GAT, was recovered as described previously (15). It was converted to the potassium salt before use.…”

Section: Methodsmentioning

confidence: 99%

Purification of myo-Inositol 1-Phosphate Synthase from Rice Cell Culture by Affinity Chromatography

Funkhouser¹,

Loewus²

1975

Plant Physiol.

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“…15 The reactions are shown in FIGURE 3. The phosphorylated glucoside of 3AT resembles AMP in its over-all structure (FIGURE 4).…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that 3-amino-1,2,4-triazole (3AT) will combine with glucose or the Cori ester to form a g1uc0side.l~ This glucoside can then be phosphorylated by hexokinase in the presence of ATP. 15 The reactions are shown in FIGURE 3. The phosphorylated glucoside of 3AT resembles AMP in its over-all structure (FIGURE 4).…”

Section: Discussionmentioning

confidence: 99%

The Origin of the Multiple Forms of Phosphorylase in Algae*

Fredrick¹

1964

Annals of the New York Academy of Sciences

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IntroductionThe enzyme phosphorylase synthesizes linear polyglucosides by the apposition of glucose residues from glucose-1-phosphate in alpha 1:4 linkages to a maltodextrin "primer." In animals this enzyme has been shown to exist in two forms: phosphorylase a, which is fully active without added adenosine-5-phosphate (AMP), and phosphorylase 6, which is inactive without the nucleotide.' Preparations of phosphorylase b can be crystallized in the presence of AMP and divalent metal ions2 This crystalline form has been shown to be a complex3:

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“…Attempts to identify compound "1" bave not yet been successful (5). ATA bas been reported to form an iron cbelate complex (7) and a glucose adduct (8). It is not at all likely, bowever, tbat compound "1" is identical witb eitber of tbese.…”

Section: Discussionmentioning

confidence: 99%