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Glucosyl-transferases, acceptor specificity

The specificity of rat-muscle glycogen-UDPglucosyl transferase has been examined by Goldemberg. A marked difference from starch-UDPglucosyl transferase is that adenosine 5- D-glucosyl pyrophosphate) is only 50% as effective as the uridine analog. In contrast to the rabbit-muscle enzyme, maltoheptaose (and maltosaccharides of DP 4, 5, 6, and 8) will slowly act as acceptors of low efficiency. Maltose and malto-triose are very inefficient acceptors, and at concentrations of 0.64 and... [Pg.400]

See other pages where Glucosyl-transferases, acceptor specificity is mentioned: [Pg.8]    [Pg.113]    [Pg.102]    [Pg.330]    [Pg.74]    [Pg.312]    [Pg.415]    [Pg.416]    [Pg.462]    [Pg.476]    [Pg.24]    [Pg.81]    [Pg.262]    [Pg.271]    [Pg.27]    [Pg.660]    [Pg.2283]    [Pg.139]    [Pg.469]    [Pg.181]    [Pg.231]    [Pg.367]    [Pg.445]    [Pg.108]    [Pg.60]   
See also in sourсe #XX -- [ Pg.219 , Pg.223 ]



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Acceptor Specificity

Glucosyl

Glucosyl acceptor

Glucosyl transferases

Glucosyl-transferases, acceptor

Glucosylation

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