123706-60-5Relevant articles and documents
Evaluating N-benzylgalactonoamidines as putative transition state analogs for β-galactoside hydrolysis
Fan, Qiu-Hua,Striegler, Susanne,Langston, Rebekah G.,Barnett, James D.
, p. 2792 - 2800 (2014/05/06)
Experimental evidence is provided for p-methylbenzyl-d-galactonoamidine to function as a true transition state analog for the enzymatic hydrolysis of aryl-β-d-galactopyranosides by β-galactosidase (A. oryzae). The compound exhibits inhibition constants in the low nanomolar concentration range (12-56 nM) for a selection of substrates. Along these lines, a streamlined synthetic method based on phase-transfer catalysis was optimized to afford the required variety of new aryl-β-d-galactopyranosides. Last, the stability of the galactonoamidines under the assay conditions was confirmed. This journal is the Partner Organisations 2014.
Synthesis, characterization, kinetic parameters, and diagnostic application of a sensitive colorimetric substrate for β-galactosidase (2-chloro-4-nitrophenyl-β-D-galactopyranoside)
Hwang,Scott
, p. 284 - 293 (2007/10/02)
The synthesis and characterization of 2-chloro-4-nitrophenyl β-D-galactopyranoside, an improved chromogenic substrate for β-galactosidase, is described. The important kinetic parameters (Km, Vmax and Kp) for this substrate were compared with those of other substrates. The diagnostic utility of this substrate in a digoxin liposome immunoassay is discussed. The new substrate offers at least four times the sensitivity enhancement as that with ortho-nitrophenyl β-D-galactopyranoside in the assays for β-galactosidase. This substrate should find use in enzyme immunoassays where βgalactosidase is used as a label. Copyright
