Glycosyltransferases are important synthetic enzymes for the construction of naturally occurring glycoconjugates as well as for the design of neoglycoconjugates. The assay methods currently available for these enzymes require tedious and time-consuming procedures for separation of products and do no
Evaluation of Some Fluorogenic Substrates for Continuous Assay of Aminopeptidase P
β Scribed by Susan J. Hawthorne; Patrick Harriott; Jaeseung Lim; Anthony J. Turner; Brian Walker; Carvell H. Williams
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 117 KB
- Volume
- 253
- Category
- Article
- ISSN
- 0003-2697
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should possess more or less extended peptide chain. As Via a combination of chemical and enzymatic syn-a rule, S 1 and S 1 subsites accommodate the side chains thesis, new hexapeptide substrates convenient for of hydrophobic amino acids-the feature often used to use in activity assessment of several
Fluorogenic substrates based on 4-methylumbelliferone (4-MU) have been widely used for the detection of phosphatase and glycosidase activities. One disadvantage of these substrates, however, is that maximum fluorescence of the reaction product requires an alkaline pH, since 4-MU has a pK(a) approxim
## Abstract The branched glycerol analogs **1** and **2** were prepared. Monoβester derivatives of these triols undergo a chromogenic or fluorogenic reaction in the presence of NaIO~4~. In contrast, both the diesters and the triols are themselves not chromogenic or fluorogenic. Diester derivatives