Lipocalin-1 is the acceptor protein for phospholipid transfer protein in tears.

Phospholipid transfer protein, ∼80 kDa, transfers phospholipids from micelles to lipid binding proteins. The acceptor protein in plasma is apolipoprotein-A1, 28 kDa. Previously, phospholipid transfer protein was found in tears but an acceptor protein was not identified.

Methods toward simplification of time resolved fluorescence anisotropy in proteins labeled with NBD (4-chloro-7-nitrobenzofurazan) adducts.

The analysis of time resolved fluorescence anisotropy for NBD tagged proteins is difficult when multiple exponential components arise from heterogeneous amino acid fluorescent adducts. Two approaches were taken toward simplification. First, N terminal selective labeling of tear lipocalin with NBD-Cl was attempted at pH 7.

Ligand binding studies by high speed centrifugal precipitation and linear spectral summation using ultraviolet-visible absorption spectroscopy.

In ligand-protein binding experiments the major challenge is to separate bound from free ligand. Equilibrium and gel filtration separation techniques are often hampered by competition for the ligand and non-specific binding. Biophysical assays have attempted to circumvent this problem using titration calorimetry and spectroscopic methods.

Ligand binding complexes in lipocalins: Underestimation of the stoichiometry parameter (n).

The stoichiometry of a ligand binding reaction to a protein is given by a parameter (n). The value of this parameter may indicate the presence of protein monomer or dimers in the binding complex. Members of the lipocalin superfamily show variation in the stoichiometry of binding to ligands.

Data on Orphan tear lipid analogs, synthesis and binding to tear lipocalin.

Data found in this article include the structures of the orphan tear lipids and their analogs that are binding candidates to tear lipocalin, the mass spectrum of products of collision induced dissociation of putative synthesized compounds of synthesized (O-oleoyl)-16 hydroxypalmitic acid. These data and analyses support the research article "Interaction of ceramides and tear lipocalin" Glasgow et al. (2018) [1].