A green, facile, one-pot synthesis of well-defined Au NPs@POM-GNSs tricomponent nanohybrids is reported (POM stands for polyoxometalate and GNSs for graphene nanosheets). The synthesis is convenient, rapid and environmentally friendly. The POMs serve as both reducing, encapsulating molecules, and bridging molecules; this avoids the introduction of other organic toxic molecules. Characterization using transmission electron microscopy, X-ray diffraction, X-ray photoelectron spectroscopy, and Raman spectroscopy analysis is performed, and the structure of the prepared nanohybrids of Au NPs@POM-GNSs is verified. Most importantly, the amperometric measurements show the Au NPs@POM-GNSs nanohybrids have high catalytic activity with good sensitivity, good long-term stability, wide linear range, low detection limit, and fast response towards H(2)O(2) detection for application as an enzyme-free biosensor. Transformation of the POMs during H(2)O(2) detection does not affect the catalytic activities of the nanohybrids. Thus, the synergistic effect of Au NPs and GNSs in the nanohybrids leads to the enhanced catalytic property.
Polo-like kinases (Plks) are a family of serine/threonine protein kinases that have been activated through phosphorylation. The activity of these kinases has been shown to be required for regulating multiple stages of mitotic progression in somatic cells. In this experiment, the changes in Plk1 expression were detected in mouse oocytes through Western blotting. The subcellular localization of Plk1 during oocyte meiotic maturation, fertilization, and early cleavage as well as after antibody microinjection or microtubule assembly disturbance was studied by confocal microscopy. The quantity of Plk1 protein remained stable during meiotic maturation and decreased gradually after fertilization. Plk1 was localized to the spindle poles of both meiotic and mitotic spindles at the early M phase and then translocated to the middle region. At anaphase and telophase, Plk1 was concentrated at the midbody of cytoplasmic cleavages. Plk1 was concentrated between the male and female pronuclei after fertilization. Plk1 disappeared at the spindle region when microtubule formation was inhibited by colchicine or staurosporine, while it was concentrated as several dots in the cytoplasm after taxol treatment. Plk1 antibody injection decreased the germinal vesicle breakdown rate and distorted MI spindle organization. Our results indicate that Plk1 is a pivotal regulator of microtubule organization during mouse oocyte meiosis, fertilization, and cleavage and that its functions may be regulated by other kinases, such as staurosporine-sensitive kinases.
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