Koshland's Reagent 1
Koshland's Reagent 1 structure
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Common Name | Koshland's Reagent 1 | ||
|---|---|---|---|---|
| CAS Number | 772-33-8 | Molecular Weight | 232.031 | |
| Density | 1.8±0.1 g/cm3 | Boiling Point | 383.0±32.0 °C at 760 mmHg | |
| Molecular Formula | C7H6BrNO3 | Melting Point | 144-149 °C(lit.) | |
| MSDS | Chinese USA | Flash Point | 185.5±25.1 °C | |
| Symbol |
GHS05 |
Signal Word | Danger | |
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Effect of protein-modifying reagents on ecto-apyrase from rat brain.
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... |
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Role of tyrosine and tryptophan in chemically modified serum albumin on its tissue distribution.
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... |
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Chemical modification of amino acid residues in glycerinated Vorticella stalk and Ca(2+)-induced contractility.
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... |
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Tyrosine and tryptophan modification monitored by ultraviolet resonance Raman spectroscopy.
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... |
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[Chemical modification of tryptophan residues of leucyl tRNA synthetase by N-bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide].
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... |
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Photocaged variants of the MunI and PvuII restriction enzymes.
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 ... |
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A conformational change associated with the phototransformation of Pisum phytochrome A as probed by fluorescence quenching.
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... |
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Effect of oxidizing agents on rabbit mammary prolactin receptors.
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... |
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Accessibility of tryptophan residues in immunoglobulin M as an index of its conformational changeability.
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... |
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Effect of 2-hydroxy-5-nitrobenzyl bromide on proton translocation by the mitochondrial H+-ATPase.
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... |