July 1974
Volume 13, Issue 7
Articles  |   July 1974
Tear Lactoferrin: A Bacteriostatic and Complexing Protein
Author Affiliations
    Department of Ophthalmology, University of Nijmegen, Nijmegen, The Netherlands
Investigative Ophthalmology & Visual Science July 1974, Vol.13, 550-554. doi:
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      R. M. BROEKHUYSE; Tear Lactoferrin: A Bacteriostatic and Complexing Protein. Invest. Ophthalmol. Vis. Sci. 1974;13(7):550-554.

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      © ARVO (1962-2015); The Authors (2016-present)

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The presence of lactoferrin in human tears is established by immunochemical techniques. Together with tear pre-albumin, IgA, and lysozyme they constitute the major tear proteins. Lactoferrin added to tears binds to IgA, IgG, and serum albumin and alters their electrophoretic mobility. On agarose and agar gels it has a different electrophoretic behavior, which together with its complexing properties offers several possibilities for misinterpretation of immunochemical results. Lactoferrin has an apparent molecular weight of approximately 82,000 as established by dodecyl sulfate-polyacrylamide gel electrophoresis. It has bacteriostatic properties, presumably due to its ability to make certain metals unavailable for microorganisms.


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