nitrophenols and cyanogen

nitrophenols has been researched along with cyanogen* in 2 studies

Other Studies

2 other study(ies) available for nitrophenols and cyanogen

Article	Year
Identification of the sites of modification on bovine carbonic anhydrase II (BCA II) by the salt-bridge reagent cyanogen, C2N2. Biochimica et biophysica acta, 1993, Jan-15, Volume: 1161, Issue:1 The hydrolase activities of bovine carbonic anhydrase B (BCA II carbonate hydrolyase, EC 4.2.1.1) were modified by cyanogen (C2N2, N identical to C-C identical to N, ethanedinitrile) with decreases in Vmax of as much as 99%. This was not accompanied by a reduction in hydrolyase activity. These changes were not reversed at lower pH values but the enzymatic activity was restored by incubation at pH 10. 14C-labeled glycine ethyl ester ([14C]GEE) specifically and covalently bound to the cyanogen-treated BCA II, as verified by HPLC and 14C monitoring. It was shown that sites of cyanogen-introduced modifications in BCA II could be effectively labeled and identified by incubation with the nucleophile [14C]GEE. Three radiolabeled tryptic peptides from BCA II arising from a labeling process designed to study cyanogen-induced modifications leading to nucleophile labile covalent bonds have been isolated. The residues identified by [14C]GEE labeling were Asp-34, Glu-117 and Asp-152. Three moieties attached to the omega-carboxyls by C2N2 were tentatively identified by molecular modeling; they were Arg-111, His-107 and/or His-119 and Ser-216, respectively. The use of C2N2 afforded a means to compare the salt bridges in two species and showed that two of three were not conserved. Topics: Amino Acids; Animals; Binding Sites; Carbonic Anhydrases; Cattle; Chromatography, High Pressure Liquid; Glycine; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Nitriles; Nitrophenols; Trypsin	1993
Irreversible inhibition of carbonic anhydrase by the carbon dioxide analog cyanogen. Biochemical and biophysical research communications, 1985, Jan-16, Volume: 126, Issue:1 Cyanogen (C2N2), a molecule with properties remarkably similar to carbon dioxide, differentially inhibits three of the four carbonic anhydrases reported here. Bovine carbonic anhydrase II shows 97% loss of esterase activity with no concommitant loss in hydratase activity. The hydratase and esterase activities of human carbonic anhydrase I are decreased by 80% and 55% respectively. Canine carbonic anhydrase shows similar results to human carbonic anhydrase I, retaining 29% hydratase and 62% esterase activity. Rabbit carbonic anhydrase sustained no loss of either hydratase or esterase activity. This inhibition occurs by an irreversible modification of the enzymes. The kinetic parameters for modified and unmodified enzymes were altered in a way that reflects the characteristic effect for each carbonic anhydrase. Topics: Acetates; Acetazolamide; Animals; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Cattle; Dogs; Humans; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Nitriles; Nitrophenols; Pyruvates; Rabbits	1985

Article

Year

Identification of the sites of modification on bovine carbonic anhydrase II (BCA II) by the salt-bridge reagent cyanogen, C2N2.

Biochimica et biophysica acta, 1993, Jan-15, Volume: 1161, Issue:1

The hydrolase activities of bovine carbonic anhydrase B (BCA II carbonate hydrolyase, EC 4.2.1.1) were modified by cyanogen (C2N2, N identical to C-C identical to N, ethanedinitrile) with decreases in Vmax of as much as 99%. This was not accompanied by a reduction in hydrolyase activity. These changes were not reversed at lower pH values but the enzymatic activity was restored by incubation at pH 10. 14C-labeled glycine ethyl ester ([14C]GEE) specifically and covalently bound to the cyanogen-treated BCA II, as verified by HPLC and 14C monitoring. It was shown that sites of cyanogen-introduced modifications in BCA II could be effectively labeled and identified by incubation with the nucleophile [14C]GEE. Three radiolabeled tryptic peptides from BCA II arising from a labeling process designed to study cyanogen-induced modifications leading to nucleophile labile covalent bonds have been isolated. The residues identified by [14C]GEE labeling were Asp-34, Glu-117 and Asp-152. Three moieties attached to the omega-carboxyls by C2N2 were tentatively identified by molecular modeling; they were Arg-111, His-107 and/or His-119 and Ser-216, respectively. The use of C2N2 afforded a means to compare the salt bridges in two species and showed that two of three were not conserved.

Topics: Amino Acids; Animals; Binding Sites; Carbonic Anhydrases; Cattle; Chromatography, High Pressure Liquid; Glycine; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Nitriles; Nitrophenols; Trypsin

1993

Irreversible inhibition of carbonic anhydrase by the carbon dioxide analog cyanogen.

Biochemical and biophysical research communications, 1985, Jan-16, Volume: 126, Issue:1

Cyanogen (C2N2), a molecule with properties remarkably similar to carbon dioxide, differentially inhibits three of the four carbonic anhydrases reported here. Bovine carbonic anhydrase II shows 97% loss of esterase activity with no concommitant loss in hydratase activity. The hydratase and esterase activities of human carbonic anhydrase I are decreased by 80% and 55% respectively. Canine carbonic anhydrase shows similar results to human carbonic anhydrase I, retaining 29% hydratase and 62% esterase activity. Rabbit carbonic anhydrase sustained no loss of either hydratase or esterase activity. This inhibition occurs by an irreversible modification of the enzymes. The kinetic parameters for modified and unmodified enzymes were altered in a way that reflects the characteristic effect for each carbonic anhydrase.

Topics: Acetates; Acetazolamide; Animals; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Cattle; Dogs; Humans; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Nitriles; Nitrophenols; Pyruvates; Rabbits

1985