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Detergent-solubilized bovine ROS (3.5 pmol of PDE6) were incubated with PrBP/δ-Sepharose (2 mg of PrBP/δ per milliliter of resin), and proteins bound to the resin (Bnd) were separated from unbound proteins (UB) by centrifugation. As a control for nonspecific binding to the resin (NS), identical samples were incubated with a large excess of PrBP/δ. Equivalent amounts of the starting sample (ROS) were also loaded. After SDS-PAGE and transfer to polyvinylidene difluoride, blots were probed with primary antibodies to GRK1, PDE6, Rab8, transducin β-subunit, and arrestin.

Journal: The Journal of Biological Chemistry

Article Title: Evaluation of the 17-kDa Prenyl-binding Protein as a Regulatory Protein for Phototransduction in Retinal Photoreceptors *

doi: 10.1074/jbc.M410475200

Figure Lengend Snippet: Detergent-solubilized bovine ROS (3.5 pmol of PDE6) were incubated with PrBP/δ-Sepharose (2 mg of PrBP/δ per milliliter of resin), and proteins bound to the resin (Bnd) were separated from unbound proteins (UB) by centrifugation. As a control for nonspecific binding to the resin (NS), identical samples were incubated with a large excess of PrBP/δ. Equivalent amounts of the starting sample (ROS) were also loaded. After SDS-PAGE and transfer to polyvinylidene difluoride, blots were probed with primary antibodies to GRK1, PDE6, Rab8, transducin β-subunit, and arrestin.

Article Snippet: Commercial antibodies to other proteins included the following: rod transducin α-subunit (K-20, Santa Cruz Biotechnology), rhodopsin (1D4, Chemicon) ( 25 ), opsin kinase (G-8, Affinity Bioreagents) ( 26 ), and Rab8 protein (Rab8, BD Biosciences).

Techniques: Incubation, Centrifugation, Binding Assay, SDS Page