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Glucosidation supported enzymes

With the establishment of the permease hypothesis, however, it was apparent that the mere formation of a complex with the mutarotase protein may be the necessary interaction in transport (15). The subsequent mutarotation could be considered to be a coincidental consequence of the complex formation. To support this idea, it was found that 1-deoxy glucose and a-methyl glucoside are excellent competitive inhibitors of the enzyme (16,61). Keston also showed that a number of cataractogenic sugars were inhibitors of lens mutarotase (62). It has since been shown that in all cases where a sugar is a substrate for the mammalian intestinal transport system it is also a competitive inhibitor of mutarotase. [Pg.282]

In support of this explanation, certain enzyme inhibitors are also inhibitors for the transport process. For example the glucoside phlorizin, which is a competitive... [Pg.486]


See other pages where Glucosidation supported enzymes is mentioned: [Pg.90]    [Pg.308]    [Pg.242]    [Pg.595]    [Pg.83]    [Pg.572]    [Pg.232]    [Pg.121]    [Pg.1464]    [Pg.345]    [Pg.120]    [Pg.331]    [Pg.307]    [Pg.69]    [Pg.397]    [Pg.253]    [Pg.125]    [Pg.130]    [Pg.356]    [Pg.357]    [Pg.241]    [Pg.242]    [Pg.394]    [Pg.505]    [Pg.578]    [Pg.578]    [Pg.582]    [Pg.377]    [Pg.265]    [Pg.275]    [Pg.251]    [Pg.22]    [Pg.69]    [Pg.240]    [Pg.94]   
See also in sourсe #XX -- [ Pg.262 ]




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Enzymes glucosidation

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