Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1992 May;9(5):629-35.
doi: 10.1023/a:1015897909739.

Adsorption of fluorescein dyes on albumin microspheres

Affiliations
Free article

Adsorption of fluorescein dyes on albumin microspheres

K Egbaria et al. Pharm Res. 1992 May.
Free article

Abstract

The surface characteristics of bovine and egg albumin microspheres were examined using four anionic dyes; sodium fluorescein, eosin, erythrosin, rose bengal, and the cationic dye rhodamine B. The adsorption isotherms of the dyes on unloaded albumin microspheres exhibited Langmuir behavior for dilute solutions of rose bengal, erythrosin, and eosin, suggesting monolayer formation in the initial stages of the sorption process. The adsorption capacity of the microspheres for the dyes (k2) and the affinity constants of the dyes for the microspheres (k1) were found to depend on both the polarizability and the hydrophobic properties of the dye, presumably reflecting the heterogeneous character of the microsphere surface. Further, the extent of sorption at higher dye concentrations was found to depend on the ability of the dye to form stable aggregates inside the microspheres and on environmental long-range forces acting at these sites. At both low and high dye concentrations, the amount adsorbed to the microsphere surface increased with increasing hydrophobicity of the dyes. The lowest adsorption was observed for the nonsubstituted dye fluorescein, whereas the most hydrophobic dye used, rose bengal, was completely adsorbed onto the microsphere surface. The data suggest that the bovine albumin microsphere surfaces are highly hydrophobic and less porous than egg albumin microsphere surfaces.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Eur J Cancer. 1974 Nov;10(11):695-700 - PubMed
    1. Proc Natl Acad Sci U S A. 1970 Apr;65(4):1057-63 - PubMed
    1. Proc Natl Acad Sci U S A. 1979 May;76(5):2128-32 - PubMed
    1. J Pharm Sci. 1992 Feb;81(2):186-90 - PubMed
    1. Eur J Cancer. 1974 Jul;10(7):405-11 - PubMed