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Welcome to the Network for Aesthetic Interpretation of Visual Art (NAIVA) website. Founded in 1998, NAIVA is a Los Angeles-based international organization dedicated to the advancement of the field of interpretation, specifically through the use of scientific and empirical evidence. We are committed to encouraging critical thinking, fostering aesthetic growth, and improving aesthetic experiences through research, theory, and the application of scientific methodology.Solubilization and purification of the substrate-binding subunit of the multidrug efflux pump NorA from Escherichia coli.

The antimicrobial efflux pump NorA from Escherichia coli is comprised of a cytoplasmic binding protein (NorB) and a periplasmic membrane fusion protein (NorC). The periplasmic domain of NorB is encoded by the norB gene and the cytoplasmic domain is derived from the norC gene. The expressed norB gene was functionally expressed in E. coli. The recombinant protein was purified by anion exchange chromatography, and an interaction with norC was demonstrated. SDS-PAGE analysis showed a 55 kDa protein band, which corresponded to the predicted molecular mass of 54.2 kDa. The purified NorB was used to develop an ELISA. Antibodies were raised against the purified protein in rabbits and rat, and a competitive ELISA was developed. The ELISA was used to detect the native NorB. The antibodies gave a minimal cross-reaction against purified NorC, but not with the binding protein of AcrAB-TolC from Pseudomonas aeruginosa, suggesting that the binding protein NorB of E. coli is a specific substrate-binding protein for the E. coli NorA 0b46394aab

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