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Mechanism-based inactivation of rat liver cytochrome P-450 2B1 by 2-methoxy-5-nitrobenzyl bromide.
Armstrong AP, Hollenberg PF. Armstrong AP, et al. Drug Metab Dispos. 1999 Jun;27(6):741-5. Drug Metab Dispos. 1999. PMID: 10348806
Mechanism-based inactivators serve as probes of enzyme mechanism, function, and structure. Koshland's Reagent II (2-methoxy-5-nitrobenzyl bromide, KR-II) is a potential mechanism-based inactivator of enzymes that perform O-dealkylations. ...
Mechanism-based inactivators serve as probes of enzyme mechanism, function, and structure. Koshland's Reagent II (2-methoxy- …
Nerve growth factor receptor binding. Influence of enzymes, ions, and protein reagents.
Banerjee SP, Cuatrecasas P, Snyder SH. Banerjee SP, et al. J Biol Chem. 1975 Feb 25;250(4):1427-33. J Biol Chem. 1975. PMID: 803504 Free article.
Receptor binding is greatly reduced by treating membranes with 2-hydroxy-5-nitrobenzyl bromide, 2-methoxy-5-nitrobenzyl bromide, diazonium tetrazole, and tetranitromethane. ...
Receptor binding is greatly reduced by treating membranes with 2-hydroxy-5-nitrobenzyl bromide, 2-methoxy-5-nitroben
Mapping of gonadotropin-releasing hormone receptor binding site.
Keinan D, Hazum E. Keinan D, et al. Biochemistry. 1985 Dec 17;24(26):7728-32. doi: 10.1021/bi00347a034. Biochemistry. 1985. PMID: 3004562
Tryptophan is another constituent that participates in the GnRH binding site, as pretreatment of pituitary membranes with 2-methoxy-5-nitrobenzyl bromide inhibited the binding (IC50 = 0.22 mM) by decreasing receptor affinity. In addition, the na …
Tryptophan is another constituent that participates in the GnRH binding site, as pretreatment of pituitary membranes with 2-methox
Chemical modification of mouse interferons.
Rusckowski M, Paucker M, Dalton B, Ogburn CA. Rusckowski M, et al. J Interferon Res. 1982;2(2):177-85. doi: 10.1089/jir.1982.2.177. J Interferon Res. 1982. PMID: 6181175
Modification of cysteine residues with 5,5'-dithio-bis (2-nitrobenzoic acid) showed an enhancement of antiviral activity of MuIFN-alpha but a gradual decrease in all activities of MuIFN-beta. Modification of tryptophan residues with 2-methoxy-5-nitrobenzyl
Modification of cysteine residues with 5,5'-dithio-bis (2-nitrobenzoic acid) showed an enhancement of antiviral activity of MuIFN-alpha but …