Compounds > diethyl pyrocarbonate

diethyl pyrocarbonate and 4-hydroxymercuribenzoate

diethyl pyrocarbonate has been researched along with 4-hydroxymercuribenzoate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19902 (50.00)18.7374
1990's1 (25.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Beale, SI; Cornejo, J1
Acebal, C; Arche, R; Estrada, P1
Acebal, C; Castillón, MP; de la Mata, I; Domínguez, JM; Macarrón, R1
George, SP; Rao, MB1

Other Studies

4 other study(ies) available for diethyl pyrocarbonate and 4-hydroxymercuribenzoate

ArticleYear
Algal heme oxygenase from Cyanidium caldarium. Partial purification and fractionation into three required protein components.
    The Journal of biological chemistry, 1988, Aug-25, Volume: 263, Issue:24

    Topics: Catalase; Chromatography; Chromatography, DEAE-Cellulose; Chromatography, Gel; Diethyl Pyrocarbonate; Ferredoxins; Heme Oxygenase (Decyclizing); Hydroxymercuribenzoates; Mixed Function Oxygenases; Molecular Weight; NADH Dehydrogenase; NADP; NADPH-Ferrihemoprotein Reductase; Rhodophyta; Spectrophotometry; Substrate Specificity

1988
Mechanism of the reaction catalyzed by acyl-CoA: lysolecithin acyltransferase from rabbit lung. pH studies and chemical modification.
    International journal of peptide and protein research, 1985, Volume: 25, Issue:5

    Topics: 1-Acylglycerophosphocholine O-Acyltransferase; Acyltransferases; Animals; Diethyl Pyrocarbonate; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Iodoacetates; Iodoacetic Acid; Isoflurophate; Kinetics; Lung; Microsomes; Rabbits; Solvents; Substrate Specificity; Thermodynamics

1985
Chemical modification of beta-glucosidase from Trichoderma reesei QM 9414.
    Journal of biochemistry, 1993, Volume: 114, Issue:5

    Topics: beta-Glucosidase; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Histidine; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Kinetics; Quinolines; Spectrophotometry, Ultraviolet; Trichoderma

1993
Conformation and polarity of the active site of xylanase I from Thermomonospora sp. as deduced by fluorescent chemoaffinity labeling. Site and significance of a histidine residue.
    European journal of biochemistry, 2001, Volume: 268, Issue:10

    Topics: Actinomycetales; Affinity Labels; Amino Acids; Binding Sites; Circular Dichroism; Cysteine; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Dose-Response Relationship, Drug; Enzyme Activation; Ethylmaleimide; Histidine; Hydroxymercuribenzoates; Indicators and Reagents; Kinetics; Lysine; Models, Chemical; o-Phthalaldehyde; Protease Inhibitors; Protein Binding; Protein Conformation; Sequence Analysis, Protein; Spectrometry, Fluorescence; Sulfhydryl Reagents; Time Factors; Trinitrobenzenesulfonic Acid; Urea; Xylan Endo-1,3-beta-Xylosidase; Xylosidases

2001