Literature DB >> 2631792

The catalysis of protein and nucleic acid coupling to an affinity membrane substrate.

A J Weiss1, S A McElhinney, L A Blankstein.   

Abstract

With the model ligands studies, which included IgG, HSA, streptavidin, MEA and amine-modified DNA, it was possible to enhance the rate of covalent immobilization by using nucleophilic acylation reaction catalysts. Imidazole, triazole and 2-hydroxypyridine are readily available catalysts that are effective when immobilizing immunoglobins. 4-N,N,Dimethylaminopyridine (DMAP) as a co-reactant or as a prereactant is a potent rate enhancer with all of the molecules that were examined. The precise protocol to be used is probably best derived empirically. In addition to optimizing the amount of ligand bound or the amount of time necessary to bind a fixed quantity of ligand, it is likely that the retained functionality of the ligand may be affected by the use of reaction catalysts.

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Year:  1989        PMID: 2631792

Source DB:  PubMed          Journal:  Biotechniques        ISSN: 0736-6205            Impact factor:   1.993


  2 in total

1.  Screening for in vivo protein-protein interactions.

Authors:  F J Germino; Z X Wang; S M Weissman
Journal:  Proc Natl Acad Sci U S A       Date:  1993-02-01       Impact factor: 11.205

2.  Dipstick enzyme immunoassay to detect Fusarium T-2 toxin in wheat.

Authors:  S De Saeger; C Van Peteghem
Journal:  Appl Environ Microbiol       Date:  1996-06       Impact factor: 4.792

  2 in total

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