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Effect of Adsorbed Proteins on the Wettability of Hydrophilic and Hydrophobic Solids

Abstract

WHEN barium stearate or other hydrophobia powders are exposed to blood plasma they remove certain coagulation factors such as factor V1 and fibrinogen2, and their surface becomes hydrophilic. Barium sulphate, aluminium hydroxide and other hydrophilic particles adsorb other coagulation factors preferentially (prothrombin, factors VII, IX and X), but changes of wettability at their surface are less obvious. To indicate if one protein may have areas of less polarity by which it can attach itself to less-wettable substrates, leaving its more polar sites exposed, and vice versa, the relative wettability of thrombin and fibrinogen adsorbed on to glass and lucite was observed as follows.

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References

  1. Vroman, L., J. Mt. Sinai Hosp., 25, 261 (1958).

    CAS  Google Scholar 

  2. Vroman, L., thesis, Utrecht (1958).

  3. Lorand, L., Brannen, jun., W. T., and Rule, N. G., Arch. Biochem. Biophys., 96, 147 (1962).

    Article  CAS  Google Scholar 

  4. Rothen, A., Ann. New York Acad. Sci., 53, 1054 (1951).

    Article  ADS  Google Scholar 

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VROMAN, L. Effect of Adsorbed Proteins on the Wettability of Hydrophilic and Hydrophobic Solids. Nature 196, 476–477 (1962). https://doi.org/10.1038/196476a0

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