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Glucose-6-phosphatase purification

Shaw (115) reported a 300-fold purification of enzyme from tobacco leaves. Activity of the enzyme was optimal at pH 5.5-5.7, and divalent cations were not required for activity. The enzyme possessed high activity toward ribonucleoside 2 - and 5 -monophosphates and glucose 1-phosphate. There was no activity toward RNA or phosphodiesters. Fluoride acts as a noncompetitive inhibitor for this enzyme. This behavior of fluoride is in contrast to the behavior with prostatic acid phosphatase where the inhibition is strictly competitive. [Pg.497]

The isolation and partial purification of soluble glucose-6-phosphatase... [Pg.553]

See other pages where Glucose-6-phosphatase purification is mentioned: [Pg.203]    [Pg.338]    [Pg.553]    [Pg.554]    [Pg.568]    [Pg.80]    [Pg.440]    [Pg.94]    [Pg.222]    [Pg.319]    [Pg.63]    [Pg.91]    [Pg.640]   
See also in sourсe #XX -- [ Pg.553 ]

See also in sourсe #XX -- [ Pg.93 ]



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Glucose-6-phosphatase

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