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Alkaline phosphatase inhibition amino acids

The enzymes used to generate reactive quinone methides often undergo inactivation by addition of this electrophile to essential nucleophilic amino acid side chains of the protein catalyst. This is a type of suicide enzyme inhibition.80 This was observed for the acid phosphatase and ribonuclease catalysts used to generate 43.76 79 Alkaline phosphatase has been used to remove the phosphate protecting group from a derivative of an o-difluoromethyl phenyl phosphate that was covalently attached to a solid support. Breakdown of the immobilized 4-hydroxybenzyl difluoride gives an immobilized quinone methide that, in principle, will react irreversibly with proteins and lead to their attachment to the solid support.81... [Pg.58]

Amino acids have been studied in relation to alkaline phosphatase, and organ differences have been observed by Bodansky (B30) and Fishman (F13). Inhibition is competitive in nature. The most recent study on the influence of L-histidine demonstrates alteration in the pH optimum (B33) of hydrolysis. Moreover, a survey of amino acid inhibitors (Fll) has produced (F13) the unique stereospecific uncompetitive inhibitor, l-phenylalanine, which is discussed in detail in section 3.1.6. [Pg.279]


See other pages where Alkaline phosphatase inhibition amino acids is mentioned: [Pg.186]    [Pg.342]    [Pg.472]    [Pg.1020]    [Pg.363]    [Pg.606]    [Pg.249]    [Pg.310]    [Pg.37]    [Pg.398]    [Pg.142]   
See also in sourсe #XX -- [ Pg.280 ]




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