Compounds > potassium chloride
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potassium chloride and 1,5-i-aedans

potassium chloride has been researched along with 1,5-i-aedans in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19902 (50.00)18.7374
1990's2 (50.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Onishi, H; Watanabe, S1
Marston, SB1
Khaitlina, S; Moraczewska, J; Mossakowska, M; Strzelecka-Golaszewska, H1
Kasprzak, AA1

Other Studies

4 other study(ies) available for potassium chloride and 1,5-i-aedans

ArticleYear
Structural and functional organization of gizzard myosin molecules: proteolytic digestion and N-iodo-acetyl-N-(5-sulfo-1-naphthyl)ethylene diamine modification.
    Advances in biophysics, 1985, Volume: 19

    Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Calcium; Calcium-Transporting ATPases; Chickens; Chymotrypsin; Enzyme Activation; Gizzard, Avian; Molecular Weight; Myosins; Naphthalenesulfonates; Papain; Peptides; Potassium Chloride; Protein Conformation; Sulfhydryl Compounds

1985
The rates of formation and dissociation of actin-myosin complexes. Effects of solvent, temperature, nucleotide binding and head-head interactions.
    The Biochemical journal, 1982, May-01, Volume: 203, Issue:2

    Topics: Actins; Adenosine Diphosphate; Adenylyl Imidodiphosphate; Animals; Binding Sites; Glycols; Kinetics; Macromolecular Substances; Myosins; Naphthalenesulfonates; Potassium Chloride; Protein Binding; Rabbits; Spectrometry, Fluorescence; Temperature

1982
Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions.
    The Biochemical journal, 1993, Feb-01, Volume: 289 ( Pt 3)

    Topics: Actins; Adenosine Triphosphate; Animals; Cysteine; Fluorescent Dyes; Macromolecular Substances; Magnesium; Naphthalenesulfonates; Peptide Fragments; Potassium Chloride; Protein Conformation; Rabbits; Scattering, Radiation; Spectrometry, Fluorescence; Sulfhydryl Reagents; Trypsin

1993
Myosin subfragment 1 inhibits dissociation of nucleotide and calcium from G-actin.
    The Journal of biological chemistry, 1993, Jun-25, Volume: 268, Issue:18

    Topics: Actins; Animals; Binding Sites; Calcium; Ethenoadenosine Triphosphate; Fluorescent Dyes; Hydrolysis; Kinetics; Myosin Subfragments; Naphthalenesulfonates; Potassium Chloride; Rabbits

1993