Page last updated: 2024-08-21

4-hydroxymercuribenzoate and trinitrobenzenesulfonic acid

4-hydroxymercuribenzoate has been researched along with trinitrobenzenesulfonic acid in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
George, SP; Rao, MB	1
Jagtap, S; Rao, M	1

Other Studies

2 other study(ies) available for 4-hydroxymercuribenzoate and trinitrobenzenesulfonic acid

Article	Year
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
Conformation and microenvironment of the active site of a low molecular weight 1,4-beta-D-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues. Biochemical and biophysical research communications, 2006, Aug-25, Volume: 347, Issue:2 Topics: Actinomycetales; Binding Sites; Carboxymethylcellulose Sodium; Circular Dichroism; Cysteine; Dose-Response Relationship, Drug; Enzyme Activation; Glucan 1,4-beta-Glucosidase; Hydroxymercuribenzoates; Kinetics; Lysine; Molecular Sequence Data; Molecular Weight; Protein Conformation; Sequence Alignment; Substrate Specificity; Trinitrobenzenesulfonic Acid	2006

Article

Year

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

Conformation and microenvironment of the active site of a low molecular weight 1,4-beta-D-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues.

Biochemical and biophysical research communications, 2006, Aug-25, Volume: 347, Issue:2

Topics: Actinomycetales; Binding Sites; Carboxymethylcellulose Sodium; Circular Dichroism; Cysteine; Dose-Response Relationship, Drug; Enzyme Activation; Glucan 1,4-beta-Glucosidase; Hydroxymercuribenzoates; Kinetics; Lysine; Molecular Sequence Data; Molecular Weight; Protein Conformation; Sequence Alignment; Substrate Specificity; Trinitrobenzenesulfonic Acid

2006