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Ni-doped TiO2 film catalysts were prepared by a plasma electrolytic oxidation (PEO) method and were mainly characterized by means of SEM, EDS, XRD, XPS, and DRS, respectively. The effects of Ni doping on the structure, composition and optical absorption property of the film catalysts were investigated along with their inherent relationships. The results show that the film catalyst is composed of anatase and rutile TiO2 with microporous structure. Doping Ni changes the phase composition and the lattice parameters (interplanar crystal spacing and cell volume) of the films. The optical absorption range of TiO2 film gradually expands and shifts to the red with increasing dosages. Both direct and indirect transition band gaps of the TiO2 films are deduced consequently. Moreover, the photocatalytic activity of the film catalysts for splitting Na2S+Na2SO3 solution into H2 is enhanced by doping with an appropriate amount of Ni. The as-prepared TiO2 film catalyst doping with 10 g/L of Ni(Ac)2 presents the highest photocatalytic reducing activity.

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The fidelity of protein transport in the secretory pathway relies on the accurate sorting of proteins to their correct destinations. To deepen our understanding of the underlying molecular mechanisms, it is important to develop a robust approach to systematically reveal cargo proteins that depend on specific sorting machinery to be enriched into transport vesicles. Here, we used an in vitro assay that reconstitutes packaging of human cargo proteins into vesicles to quantify cargo capture. Quantitative mass spectrometry (MS) analyses of the isolated vesicles revealed cytosolic proteins that are associated with vesicle membranes in a GTP-dependent manner. We found that two of them, FAM84B (also known as LRAT domain containing 2 or LRATD2) and PRRC1, contain proline-rich domains and regulate anterograde trafficking. Further analyses revealed that PRRC1 is recruited to endoplasmic reticulum (ER) exit sites, interacts with the inner COPII coat, and its absence increases membrane association of COPII. In addition, we uncovered cargo proteins that depend on GTP hydrolysis to be captured into vesicles. Comparing control cells with cells depleted of the cargo receptors, SURF4 or ERGIC53, we revealed specific clients of each of these two export adaptors. Our results indicate that the vesicle formation assay in combination with quantitative MS analysis is a robust and powerful tool to uncover novel factors that mediate vesicular trafficking and to uncover cargo clients of specific cellular factors.