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Journal ArticleDOI

The Stability of N-Ethylmaleimide and its Reaction with Sulfhydryl Groups

John Delafield Gregory
- 01 Jul 1955 - 
- Vol. 77, Iss: 14, pp 3922-3923
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This article is published in Journal of the American Chemical Society.The article was published on 1955-07-01. It has received 336 citations till now.

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Using "click" chemistry to prepare SAM substrates to study stem cell adhesion.

TL;DR: The results demonstrate that CuAAC is a suitable mechanism for conjugating peptides to otherwise bioinert SAMs and the resulting SAMs can be used to study the dependence of peptide density on stem cell behavior.
Book ChapterDOI

Glutamine Synthetase of Escherichia Coli: Some Physical and Chemical Properties

TL;DR: This chapter discusses some aspects of the macromolecular structure of glutamine synthetase from Escherichia coli, together with some interactions of the enzyme with effectors, and justifies a detailed consideration of the presently known structural features of this enzyme.
Journal ArticleDOI

Switchable fluorescence of gold nanoclusters for probing the activity of alkaline phosphatase and its application in immunoassay.

TL;DR: A novel "switch-on" fluorescent assay for probing the activity of alkaline phosphatase (ALP) is developed with a detection limit as low as 0.002 U/L and paves a new way to develop convenient, sensitive, and selective metal NCs-based fluorescent "turn- on" probes with promising applications in versatile biosensing.
Journal ArticleDOI

Catalysis of imido group hydrolysis in a maleimide conjugate

TL;DR: A chromophoric maleimide is used to demonstrate that both molybdate and chromate catalyze the hydrolysis of an imido group near neutral pH, and provides a strategy for decreasing the heterogeneity of bioconjugates derived from maleimides.
Journal ArticleDOI

d-Amino Acid Oxidase III. STUDIES OF FLAVIN ADENINE DINUCLEOTIDE BINDING

TL;DR: These inhibition studies indicated that the adenosine moiety and the pyrophosphate group of the FAD molecule contributed to the effective binding of FAD to d-amino acid oxidase.
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