Literature DB >> 8024564

Photocleavable nitrobenzyl-protein conjugates.

S Thompson1, J A Spoors, M C Fawcett, C H Self.   

Abstract

We have developed methods to allow the reversible binding of up to 15 nitrobenzyl residues per bovine serum albumin molecule and show 95% of these residues can be removed by exposure to UV light for 10 min. The general non-specific coating method is presented by means of a model system but is applicable to a wide range of proteins with important biological functions. Potentially, any protein could be coated with sufficient photo-removable groups to inhibit its biological function. Its activity may then be restored at will by exposure to UV light removing the coupled 2-nitrobenzyl groups.

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Year:  1994        PMID: 8024564     DOI: 10.1006/bbrc.1994.1834

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Hydrophobic Tags for Highly Efficient Light-Activated Protein Release.

Authors:  Karthik Nadendla; Bhagyesh R Sarode; Simon H Friedman
Journal:  Mol Pharm       Date:  2019-05-31       Impact factor: 4.939

2.  Optical Control of Antibody Activity by Using Photocleavable Bivalent Peptide-DNA Locks.

Authors:  Simone F A Wouters; Elvira Wijker; Maarten Merkx
Journal:  Chembiochem       Date:  2019-09-03       Impact factor: 3.164

  2 in total

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