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转载至Experimental evidence for the ubiquitin proteasome pathway in human sperm.
Urokinase-type plasminogen activator and the mitotic regulatory protein p34(cdc2) are degraded by the ubiquitin proteasome pathway in proliferating mammalian cells. Previous studies have shown that mouse spermatogonia contain a protein which copurifies with p34(cdc2) and is capable of degrading both proteins. This study shows that human sperm also contain a p34(cdc2)-binding protein. Human sperm extract, but not mouse sperm extract, binds to a monoclonal antibody directed against the p34(cdc2) N-terminus. Western blotting demonstrates that the N-terminus of p34(cdc2) is ubiquitinated and degraded by proteasomes in vitro, and that sperm contain active ubiquitin ligase. These results are consistent with the recent cloning of the human cdc2 homolog gene (MESR1) and the presence of a p34(cdc2) ortholog in human and mouse. The existence of the ubiquitin proteasome pathway in human sperm suggests that ubiquitin ligase activity may play a role in the regulation of the proliferative potential of human sperm.The effects of nuclear structure on the low-energy β-reactions of the Au(i)-doped silylene cluster [{Au4(η(1)-C8H8)}2(tBuNC)2].
The Au(i)-doped silylene cluster [{Au4(η(1)-C8H8)}2(tBuNC)2] (2) has been synthesized by the reaction of 1-methyl-1,3-dichloro-2,2-bis(trimethylsilyl)ethene (6) with bis(triphenylphosphine)gold(I) tetrafluoroborate. Compound 2 was characterized by its NMR and IR spectra. Its solution behavior was studied by UV-vis absorption spectroscopy. The results of quantum chemical calculation showed that the possible reaction pathways of 2 are β-H elimination from the silylene ligands to the gold center, isomerization from the silylene ligands to the gold center, and α-elimination of a gold atom to

 

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System Requirements:

* Windows 7/8/8.1/10 (64-bit)
* 1.2 GHz Dual-core processor (or higher)
* 3 GB RAM (4 GB recommended)
* 6 GB available hard disk space
* 1280×800 (1280×1024) resolution display
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