lysine has been researched along with 2,6-mansyl chloride in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 4 (80.00) | 18.7374 |
1990's | 1 (20.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Hiratsuka, T | 1 |
Burtnick, LD; Isaac, CD | 1 |
Hiratsuka, T; Uchida, K | 2 |
dos Remedios, CG; Hambly, BD; Huang, W; Kekic, M; Moens, PD | 1 |
5 other study(ies) available for lysine and 2,6-mansyl chloride
Article | Year |
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Reduction in the actin-activated ATPase activity of cardiac myosin induced by fluorescence labeling of two reactive lysyl residues located in its subfragment-1/subfragment-2 link region.
Topics: Actins; Actomyosin; Adenosine Triphosphatases; Anilino Naphthalenesulfonates; Animals; Ca(2+) Mg(2+)-ATPase; Enzyme Activation; Fluorescent Dyes; Kinetics; Lysine; Macromolecular Substances; Molecular Weight; Myocardium; Myosins; Protein Binding | 1981 |
Modification of actin with 2-(N-methylanilino)naphthalene-6-sulfonyl chloride.
Topics: Actins; Anilino Naphthalenesulfonates; Animals; Cysteine; Deoxyribonucleases; Fluorescent Dyes; Lysine; Potassium Chloride; Protein Binding; Rabbits; Spectrometry, Fluorescence; Viscosity | 1984 |
Lysyl residues of cardiac myosin accessible to labeling with a fluorescent reagent, N-methyl-2-anilino-6-naphthalenesulfonyl chloride.
Topics: Adenosine Triphosphatases; Anilino Naphthalenesulfonates; Animals; Fluorescent Dyes; Lysine; Metals; Myocardium; Myosins; Peptide Fragments; Peptide Hydrolases; Peptides; Protein Conformation; Swine | 1980 |
Localization and isolation of the peptides in cardiac myosin that contain the lysyl residues accessible to labeling with a fluorescent reagent, N-methyl-2-anilino-6-naphthalenesulfonyl chloride.
Topics: Anilino Naphthalenesulfonates; Animals; Chymotrypsin; Fluorescent Dyes; Heart Ventricles; Lysine; Macromolecular Substances; Molecular Weight; Myocardium; Myosins; Peptide Fragments; Peptides; Swine | 1981 |
Distance measurements near the myosin head-rod junction using fluorescence spectroscopy.
Topics: Allosteric Site; Anilino Naphthalenesulfonates; Animals; Binding Sites; Biophysical Phenomena; Biophysics; Chickens; Cysteine; Energy Transfer; Fluorescent Dyes; In Vitro Techniques; Lysine; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Myosin Subfragments; Rabbits; Spectrometry, Fluorescence; Swine; Thermodynamics | 1996 |