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Related Concept Videos

Labeling DNA Probes03:31

Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...

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Updated: Jul 24, 2026

Multiplexed Fluorescent Microarray for Human Salivary Protein Analysis Using Polymer Microspheres and Fiber-optic Bundles
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A fluorescent probe study of salmine AI.

S F Russo, R G Engel

    Physiological Chemistry and Physics
    |January 1, 1978
    PubMed
    Summary

    This study used the 1-p-toluidinylnapthalene-8-sulfonate (1,8-TNS) fluorescent probe to identify moderately nonpolar binding sites on salmine AI. Findings reveal cooperative binding influenced by ionic strength and acidity.

    Area of Science:

    • Biochemistry
    • Biophysical Chemistry

    Background:

    • Salmine AI is a protamine, a small, arginine-rich protein.
    • Understanding protein-ligand interactions is crucial in molecular biology and drug discovery.

    Purpose of the Study:

    • To investigate the nonpolar binding sites on salmine AI using a fluorescent probe.
    • To characterize the binding interactions between salmine AI and 1,8-TNS.

    Main Methods:

    • Fluorescence spectroscopy utilizing 1-p-toluidinylnapthalene-8-sulfonate (1,8-TNS) as a probe.
    • Equilibrium dialysis and thin film dialysis to assess binding kinetics and affinity.

    Main Results:

    • 1,8-TNS exhibited fluorescence enhancement at 497-500 nm upon binding to salmine AI, indicating moderately nonpolar sites.

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  • Binding affinity decreased with increasing ionic strength (0.002 M to 0.050 M).
  • Positive cooperativity was observed in the binding of 1,8-TNS to salmine AI.
  • Conclusions:

    • Salmine AI possesses moderately nonpolar binding sites accessible to 1,8-TNS.
    • The binding interaction is sensitive to environmental factors like ionic strength and acidity.
    • Thin film dialysis offers a more rapid and stable method for studying probe-protein interactions compared to equilibrium dialysis.