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. 2018 Dec 17;116(5):1723–1732. doi: 10.1073/pnas.1817984116

Fig. 1.

Fig. 1.

Human GPIHBP1 binds to LPL with 1:1 stoichiometry, as judged by native polyacrylamide gel electrophoresis. In the absence of GPIHBP1, little LPL enters native polyacrylamide gels and does not migrate as a distinct band, simply because LPL is a very basic protein. GPIHBP1 is highly acidic; thus, an LPL–GPIHBP1 complex readily enters native gels and migrates as a distinct band. (A) Binding stoichiometry of LPL and GPIHBP1, determined by titrating 1.5 µM human LPL (lane 1) with increasing amounts of full-length human GPIHBP1 [0.3–3.0 µM full-length GPIHBP1 (GPIHBP121–151)] (lanes 2–11). The relative amounts of LPL–GPIHBP1 complexes (determined by scanning Coomassie blue-stained bands) are superimposed on the gels as black diamonds. These studies reveal a 1:1 binding stoichiometry. (B) A similar titration of 7.6 µM LPL (lane 1) with increasing amounts of a synthetic peptide corresponding to the N-terminal acidic domain of GPIHBP1 (GPIHBP121–53; 1–10 µM) (lanes 2–11). These experiments reveal 1:1 binding stoichiometry.