Abstract
Human tear fluid is a very complex mixture. The main lacrimal gland secretes a group of six proteins, the tear lipocalins, characterized by low molecular weight and an acidic pI.1 These secreted proteins are processed to differing extents at their N-terminal end, resulting in heterogeneity evidenced by multiple spots in two-dimensional electrophoresis.2,3 These tear proteins belong to the large lipocalin family4,5 of which the archetype is retinol binding protein (RBP). This is demonstrated by their amino-acid structure (176 amino-acid residues, some highly conserved amino-acid positions),3 by the corresponding cDNA structure6 and by gene structure and location.7–10 However, there is a low degree of overall homology (20–37% for amino acids and 23–30% for nucleic acids) between tear lipocalin and the other human lipocalins.
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Ressot, C., Lassagne, H., Kemeny, JL., Gachon, AM.F. (1998). Tissue Expression of Tear Lipocalin in Humans. In: Sullivan, D.A., Dartt, D.A., Meneray, M.A. (eds) Lacrimal Gland, Tear Film, and Dry Eye Syndromes 2. Advances in Experimental Medicine and Biology, vol 438. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5359-5_7
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DOI: https://doi.org/10.1007/978-1-4615-5359-5_7
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