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fluorescein-5-isothiocyanate and acetyl phosphate

fluorescein-5-isothiocyanate has been researched along with acetyl phosphate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Beaugé, L; Berberián, G1
Daiho, T; Kanazawa, T; Yamagata, K1
Hayashi, Y; Kaya, S; Taniguchi, K; Tsuda, T; Yokoyama, T1
Champeil, P; Henao, F; Lacapere, JJ; McIntosh, DB1

Other Studies

4 other study(ies) available for fluorescein-5-isothiocyanate and acetyl phosphate

ArticleYear
Phosphorylation of Na,K-ATPase by acetyl phosphate and inorganic phosphate. Sidedness of Na+, K+ and nucleotide interactions and related enzyme conformations.
    Biochimica et biophysica acta, 1991, Apr-02, Volume: 1063, Issue:2

    Topics: Animals; Cell Membrane; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescence; Fluorescent Dyes; Kidney; Liposomes; Organophosphates; Phosphates; Phosphorylation; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Swine; Thiocyanates

1991
Labeling of lysine 492 with pyridoxal 5'-phosphate in the sarcoplasmic reticulum Ca(2+)-ATPase. Lysine 492 residue is located outside the fluorescein 5-isothiocyanate-binding region in or near the ATP binding site.
    The Journal of biological chemistry, 1993, Oct-05, Volume: 268, Issue:28

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Animals; Binding Sites; Calcium-Transporting ATPases; Chromatography, High Pressure Liquid; Fluorescein-5-isothiocyanate; Hydrolysis; Lysine; Molecular Sequence Data; Organophosphates; Peptide Mapping; Pyridoxal Phosphate; Rabbits; Sarcoplasmic Reticulum

1993
ATP and acetyl phosphate induces molecular events near the ATP binding site and the membrane domain of Na+,K+-ATPase. The tetrameric nature of the enzyme.
    The Journal of biological chemistry, 1998, Sep-18, Volume: 273, Issue:38

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Affinity Labels; Animals; Cell Membrane; Dogs; Fluorescein-5-isothiocyanate; Kidney; Kinetics; Macromolecular Substances; Magnesium; Models, Structural; Organophosphates; Pyridoxal Phosphate; Sodium; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Swine; Time Factors

1998
A remarkably stable phosphorylated form of Ca2+-ATPase prepared from Ca2+-loaded and fluorescein isothiocyanate-labeled sarcoplasmic reticulum vesicles.
    The Journal of biological chemistry, 2001, Feb-23, Volume: 276, Issue:8

    Topics: Biological Transport, Active; Calcium; Calcium-Transporting ATPases; Cell Polarity; Cytosol; Enzyme Stability; Fluorescein-5-isothiocyanate; Fluorescence; Models, Chemical; Organophosphates; Phosphates; Phosphoproteins; Sarcoplasmic Reticulum; Spectrophotometry

2001