2-羟基-5-硝基溴苄

Int. J. Biochem. Cell Biol. 32(1) , 105-13, (2000)

We have tested several chemical modifiers to investigate which amino acid residues, present in the primary structure of the ecto-apyrase, could be involved in catalysis. Synaptosomes from cerebral cortex of rats were prepared and the ATP diphosphohydrolase ac...

Biol. Pharm. Bull. 29(9) , 1926-30, (2006)

To investigate the effect of functional groups in bovine serum albumin (BSA) on its tissue distribution characteristics, tyrosine (Tyr) or tryptophan (Trp) residues of BSA were chemically modified by tetranitromethane (TNM) and 2-hydroxy-5-nitrobenzyl bromide...

Cell Motil. Cytoskeleton 36(4) , 305-12, (1997)

The glycerinated stalk of the peritrich ciliate Vorticella, was treated with various reagents to chemically modify the amino acid residues. The influences of these modifcations on spasmoneme contractility were investigated. First, it was confirmed that the sp...

Biochim. Biophys. Acta 873(1) , 73-8, (1986)

Nitration of tyrosine with tetranitromethane shifts the tyrosine absorption spectrum and abolishes its 200 nm-excited resonance Raman spectrum. There is no detectable resonance Raman contribution from either reactants or products. Likewise, modification of tr...

Bioorg. Khim. 11(5) , 605-12, (1985)

The structural accessibility of tryptophan residues in leucyl-tRNA synthetase from cow mammary gland has been studied using chemical modifications by N-bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide. The modifications were monitored by UV absorbance and...

Biochemistry 50(14) , 2800-7, (2011)

Regulation of proteins by light is a new and promising strategy for the external control of biological processes. In this study, we demonstrate the ability to regulate the catalytic activity of the MunI and PvuII restriction endonucleases with light. We used ...

Biochemistry 33(3) , 708-12, (1994)

Dynamic quenching of the two lifetime component tryptophan fluorescence of Pisum phytochrome has revealed differential accessibility of certain residues. Both acrylamide and Tl+ ions showed preferential exposure of some tryptophans in Pfr-phytochrome. Greater...

Mol. Cell. Endocrinol. 46(1) , 37-42, (1986)

Treatment of rabbit mammary membrane-bound and solubilized prolactin receptors with the oxidizing agents N-chlorobenzene sulfonamide and N-bromosuccinimide resulted in total inactivation of the ability of the receptor to bind prolactin. A similar inactivation...

J. Biomol. Struct. Dyn. 8(3) , 709-20, (1990)

Demonstrated herein is the possibility of using the accessibility of tryptophan (Trp) residues in immunoglobulin M (IgM) upon modification with Koshland reagent (2-hydroxy-5-nitrobenzyl bromide) as an index of the conformational changeability of IgM. Of fourt...

Biochem. Biophys. Res. Commun. 155(1) , 130-7, (1988)

2-Hydroxy-5-nitrobenzyl bromide, a highly reactive reagent towards tryptophan residues in proteins, is shown to activate the passive proton flux through the inner mitochondrial membrane of bovine heart submitochondrial particles (ETPH). When added at low conc...