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121.
Antibodies against purified ( from the rectal gland of Squalus acanthias, as well as against its catalytic subunit, inhibited ouabain binding by as much as 50%. However, antibodies against the glycoprotein subunit did not inhibit ouabain binding. These data suggest that binding of antibody against the catalytic subunit to the enzyme either covers the ouabain binding site or destroys its conformation, while binding of antibody against the glycoprotein has no such effect. 相似文献
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Galium procurrens is described as a new diploid relic species from Montenegro/N. Albania and SW. Bulgaria. It is related to the tetraploidG. laevigatum and other diploid and polyploid taxa of theG. sylvaticum-group inhabiting European deciduous forests. 相似文献
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ZHENG LianBin LI YongLan XI HuanJiu YU KeLi LU ShunHua SHI Rui WEN YouFeng BAO JingPing ZHANG XingHua LI YuLing REN Fu XU GuoChang 《中国科学:生命科学英文版》2015,58(2):215-217,1,3
<正>Dear Editor,Shortly after initiating the"Physical Anthropological Research on Han Chinese"research project,we applied uniform sampling methods as well as methods and instruments of measurement to obtain a complete set of measurements of physical anthropological indicators among Han populations across China.Among these measurements,body stature was a key indicator.Currently,there should be reliable 相似文献
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Lee Joo-Hyoung Park Jong-Ho Park Sun-Hye Kim Sun-Hong Kim Jee Yon Min Jeong-Ki Lee Gyun Min Kim Yeon-Gu 《Applied microbiology and biotechnology》2018,102(11):4729-4739
Applied Microbiology and Biotechnology - Despite the relatively low transfection efficiency and low specific foreign protein productivity (qp) of Chinese hamster ovary (CHO) cell-based transient... 相似文献
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Longhe Xu Felipe Matsunaga Jin Xi Min Li Jingyuan Ma 《Journal of biomolecular structure & dynamics》2013,31(11):1833-1840
We recently demonstrated that the anionic detergent sodium dodecyl sulfate (SDS) specifically interacts with the anesthetic binding site in horse spleen apoferritin, a soluble protein which models anesthetic binding sites in receptors. This raises the possibility of other detergents similarly interacting with and occluding such sites from anesthetics, thereby preventing the proper identification of novel anesthetic binding sites. n-Dodecyl β-D-maltoside (DDM) is a non-ionic detergent commonly used during protein-anesthetic studies because of its mild and non-denaturing properties. In this study, we demonstrate that SDS and DDM occupy anesthetic binding sites in the model proteins human serum albumin (HSA) and horse spleen apoferritin and thereby inhibit the binding of the general anesthetics propofol and isoflurane. DDM specifically interacts with HSA (Kd?=?40?μM) with a lower affinity than SDS (Kd?=?2?μM). DDM exerts all these effects while not perturbing the native structures of either model protein. Computational calculations corroborated the experimental results by demonstrating that the binding sites for DDM and both anesthetics on the model proteins overlapped. Collectively, our results indicate that DDM and SDS specifically interact with anesthetic binding sites and may thus prevent the identification of novel anesthetic sites. Special precaution should be taken when undertaking and interpreting results from protein-anesthetic investigations utilizing detergents like SDS and DDM. 相似文献