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  • Title: Characterization of the binding of Triton X-100 to equine and rabbit serum albumin.
    Author: Sukow WW, Bailey J.
    Journal: Physiol Chem Phys; 1981; 13(5):455-9. PubMed ID: 7339636.
    Abstract:
    The binding isotherms for Triton X-100 binding to equine and rabbit serum albumin were determined by equilibrium dialysis at 16 degrees C in pH 7.0, I = 0.05 phosphate buffer. Presented in a Scatchard plot, the binding isotherms are a straight line, indicating thermodynamically independent and identical binding sites. In this model equine serum albumin is characterized as having 11 such sites with an equilibrium constant of 6.0 x 10(3) M-1. Similarly, rabbit serum albumin is characterized as having 9 such sites with an equilibrium constant of 8.0 x 10(3) M-1.
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