1-乙酰基咪唑
1-乙酰基咪唑结构式
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常用名 | 1-乙酰基咪唑 | 英文名 | 1-acetylimidazole |
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| CAS号 | 2466-76-4 | 分子量 | 110.114 | |
| 密度 | 1.1±0.1 g/cm3 | 沸点 | 222.0±23.0 °C at 760 mmHg | |
| 分子式 | C5H6N2O | 熔点 | 99-105 °C(lit.) | |
| MSDS | 中文版 美版 | 闪点 | 88.0±22.6 °C |
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Involvement of conserved histidine, lysine and tyrosine residues in the mechanism of DNA cleavage by the caspase-3 activated DNase CAD.
Nucleic Acids Res. 30(6) , 1325-32, (2002) The caspase-activated DNase (CAD) is involved in DNA degradation during apoptosis. Chemical modification of murine CAD with the lysine-specific reagent 2,4,6-trinitrobenzenesulphonic acid and the tyrosine-specific reagent N-acetylimidazole leads to inactivati... |
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Changes in the level and activation state of the plasma membrane H(+)-ATPase during aging of red beet slices.
Plant Physiol. 114(3) , 857-62, (1997) The effect of aging on the plasma membrane (PM) H(+)-ATPase of red beet (Beta vulgaris L.) parenchyma discs was analyzed in PM purified by aqueous two-phase partitioning. Aging increased both the activity in the amount of immunodetectable H(+)-ATPase in the P... |
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Chemical modification of active site residues in gamma-glutamyl transpeptidase. Aspartate 422 and cysteine 453.
J. Biol. Chem. 270(21) , 12476-80, (1995) gamma-Glutamyl transpeptidase, an enzyme of central significance in glutathione metabolism, is inactivated by iodoacetamide, which esterifies an active site carboxyl group identified here as that of Asp-422. Treatment of the inactivated enzyme with hydroxylam... |
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Chemical modification of xylanase from Trichosporon cutaneum shows the presence of carboxyl groups and cysteine residues essential for enzyme activity.
J. Protein Chem. 18(6) , 677-86, (1999) The endo-beta-1,4-xylanase (EC 3.2.1.8) from Trichosporon cutaneum was chemically modified using amino acid-specific reagents. The enzyme does not bear arginines essential for activity, since 1,2-cyclohexanedione and 2,3-butanedione, although they modify the ... |
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Chemical modification of ovine prolactin with N-acetylimidazole.
Int. J. Pept. Protein Res. 42(1) , 33-8, (1993) Reaction of ovine prolactin (oPRL) with a 150-fold molar excess of N-acetylimidazole over protein content resulted in the modification of 2.5 tyrosine residues and 1.2 lysine residues. Acetylation greatly decreased the in vitro binding capacity to lactogenic ... |
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Stability, structural and suicide inactivation changes of mushroom tyrosinase after acetylation by N-acetylimidazole.
Int. J. Biol. Macromol. 34(4) , 257-62, (2004) Modification (acetylation) of Tyr residues with N-acetylimidazole protects outstandingly mushroom tyrosinase (MT) from the suicide inactivation in the presence of its catecholic substrate, 4-[(4-methylbenzo) azo]-1,2-benzenediol. UV spectrophotometric experim... |
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Regulation of the reduced-folate transporter by nitric oxide in cultured human retinal pigment epithelial cells.
Biochem. Biophys. Res. Commun. 257(2) , 279-83, (1999) The regulation of the reduced-folate transporter (RFT) by nitric oxide (NO) was analyzed in human retinal pigment epithelial (HRPE) cells. NO inhibited specifically and reversibly the uptake of N5-methyltetrahydrofolate by a cGMP-independent mechanism. The in... |
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Specificity of aspartokinase III from Escherichia coli and an examination of important catalytic residues.
Arch. Biochem. Biophys. 335(1) , 73-81, (1996) Aspartokinase III (AK III) has been purified from a plasmid-containing strain of Escherichia coli. The enzyme shows broad specificity for the phosphoryl acceptor substrate. Structural analogs of aspartic acid with a derivatized alpha-carboxyl group are accept... |
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Conformational dependency of human IgG heavy chain-associated Gm allotypes.
Mol. Immunol. 30(4) , 341-51, (1993) Human IgG allotypic markers Gm(a)[Glm(1)], Gm(x)[Glm(2)]; Gm(f)[Glm(4)], Gm(b)[G3m(5) and (11)] and Gm(g)[G3m(21)] were studied after chemical modification of IgG histidines by diethylpyrocarbonate, tyrosines by N-acetylimidazole and lysines by formaldehyde a... |
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Structural and functional differentiation of three groups of tyrosine residues by acetylation of N-acetylimidazole in manganese stabilizing protein.
Biochemistry 44(2) , 719-25, (2005) To study its contribution to the assembly of the green plant manganese stabilizing protein (MSP) into photosystem II (PSII), tyrosine residues were specifically acetylated using N-acetylimidazole (NAI). In soluble MSP, three groups of Tyr residues could be di... |