iodoacetamide has been researched along with 1-anilino-8-naphthalenesulfonate in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (33.33) | 18.7374 |
| 1990's | 2 (33.33) | 18.2507 |
| 2000's | 2 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Takenaka, F; Takeo, S | 1 |
| Joseph, M; Nagaraj, R | 1 |
| Horowitz, P; Luduena, RF; Roach, MC | 1 |
| Barra, D; Jones, WM; Manning, JM; Scaloni, A | 1 |
| Moulin, A; Puigserver, A; Smialowski-Fléter, S; Villard, C | 1 |
| Alam, M; Gilham, D; Lehner, R; Vance, DE | 1 |
6 other study(ies) available for iodoacetamide and 1-anilino-8-naphthalenesulfonate
| Article | Year |
|---|---|
Comparison of myocardial and adipose tissue lipase activity in the rat.
Topics: Adipose Tissue; Animals; Epinephrine; Fatty Acids; Heart; In Vitro Techniques; Iodoacetamide; Isoproterenol; Lipase; Male; Myocardium; Rats; Triglycerides | 1978 |
Unfolding of lysozyme by breaking its disulphide bridges results in exposure of hydrophobic sites.
Topics: Anilino Naphthalenesulfonates; Animals; Binding Sites; Chickens; Disulfides; Fluorescent Dyes; Hydrogen-Ion Concentration; Iodoacetamide; Molecular Structure; Muramidase; Protein Denaturation; Spectrometry, Fluorescence | 1992 |
The effects of the anilinonaphthalenesulfonates on the alkylation of tubulin: correlation between the appearance of sulfhydryl groups and apolar binding sites.
Topics: Alkylation; Anilino Naphthalenesulfonates; Iodoacetamide; Protein Binding; Tubulin | 1986 |
Human acylpeptide hydrolase. Studies on its thiol groups and mechanism of action.
Topics: Amino Acid Sequence; Amino Acids; Aminopeptidases; Enzyme Reactivators; Erythrocytes; Esterases; Humans; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Iodoacetamide; Kinetics; Lactones; Lipase; Molecular Sequence Data; Peptide Hydrolases; Sulfhydryl Compounds | 1994 |
Structure-function relationships in the carboxylic-ester-hydrolase superfamily. Disulfide bridge arrangement in porcine intestinal glycerol-ester hydrolase.
Topics: Animals; Binding Sites; Carboxylic Ester Hydrolases; Cholinesterases; Cyanogen Bromide; Cysteine; Disulfides; Dithiothreitol; Enzyme Stability; Intestinal Mucosa; Iodoacetamide; Lipase; Peptide Fragments; Peptide Mapping; Protein Binding; Protein Conformation; Sequence Analysis; Structure-Activity Relationship; Substrate Specificity; Swine | 2000 |
Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase.
Topics: Acylation; Amino Acid Sequence; Animals; Binding Sites; Butyrates; Catalysis; Cell Line; Chlorocebus aethiops; COS Cells; Cysteine; Gene Deletion; Gene Expression; Humans; Hymecromone; Iodoacetamide; Lipase; Mercaptoethanol; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Phenylalanine; Point Mutation; Protein Folding; Recombinant Proteins; Sequence Homology, Amino Acid; Spodoptera; Substrate Specificity; Transfection | 2006 |