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Om P. Malhotra W.B. Rippon D.D. Solomon A.G. Walton 《International journal of biological macromolecules》1979,1(3):137-143
Structural aspects of the behaviour of prothrombin and its fragments have been examined by circulae dichroism spectroscopy. It has been noted that a correlation exists between the ellipticity of the aromatic bands and the physiological activity of partially denatured and abnormal prothrombins. The origin of these bands appears to be predominantly based in the region of one or more tyrosine residues. It is shown that whereas complexation of calcium with prothrombin causes little change in the dromatic c.d. spectrum, the effect on prothrombin fragment 1 is quite dramatic. It is concluded that the binding of calcium to the dicarboxyglutamate residues in fragment 1 causes a concomitant ionization of one or more tyrosine residues. The behaviour of fragment 1 is indicative of an intact protein with a tertiary structure which supports our previous trimodular model of prothrombin, which is activated in part by the unlocking of an ‘ionic’ lock. This lock consists of the highly negatively charged dicarboxyglutamyl patch at or near the N terminus of prothrombin and a positively charged basic patch near the C terminus. 相似文献
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Das B Rudra S Yadav A Ray A Rao AV Srinivas AS Soni A Saini S Shukla S Pandya M Bhateja P Malhotra S Mathur T Arora SK Rattan A Mehta A 《Bioorganic & medicinal chemistry letters》2005,15(19):4261-4267
Novel oxazolidinones were synthesized containing a number of substituted five-membered heterocycles attached to the 'piperazinyl-phenyl-oxazolidinone' core of eperezolid. Further, the piperazine ring of the core was replaced by other diamino-heterocycles. These modifications led to several compounds with potent activity against a spectrum of resistant and susceptible gram-positive organisms, along with the identification of ranbezolid (RBx 7644) as a clinical candidate. 相似文献
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Open-channel block by the cytoplasmic tail of sodium channel beta4 as a mechanism for resurgent sodium current 总被引:1,自引:0,他引:1
Voltage-gated sodium channels with "resurgent" kinetics are specialized for high-frequency firing. The alpha subunits interact with a blocking protein that binds open channels upon depolarization and unbinds upon repolarization, producing resurgent sodium current. By limiting classical inactivation, the cycle of block and unblock shortens refractory periods. To characterize the blocker in Purkinje neurons, we briefly exposed inside-out patches to substrate-specific proteases. Trypsin and chymotrypsin each removed resurgent current, consistent with established roles for positively charged and hydrophobic/aromatic groups in blocking sodium channels. In Purkinje cells, the only known sodium channel-associated subunit that has a cytoplasmic sequence with several positive charges and clustered hydrophobic/aromatic residues is beta4 (KKLITFILKKTREK; beta4(154-167)). After enzymatic removal of block, beta4(154-167) fully reconstituted resurgent current, whereas scrambled or point-mutated peptides were ineffective. In CA3 pyramidal neurons, which lack beta4 and endogenous block, beta4(154-167) generated resurgent current. Thus, beta4 may be the endogenous open-channel blocker responsible for resurgent kinetics. 相似文献
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Conclusions In vivo ocular availability of ketorolac was evaluated following ocular instillation of aqueous, oil, and ointment formulations
to normal corneas of rabbits and monitoring ketorolac concentration in aqueous humor by HPLC. Compared with aqueous drop,
sesame and soybean oil drops of ketorolac provided higher ocular availability followed by ophthalmic ointment. The ointment
formulation provided maximum sustained effect. Ketorolac aqueous drop with BAC and EDTA improved the rate of ocular absorption
though not the extent.
Published: October 24, 2005 相似文献
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PKCeta is required for beta1gamma2/beta3gamma2- and PKD-mediated transport to the cell surface and the organization of the Golgi apparatus
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Protein kinase D (PKD) binds to a pool of diacylglycerol (DAG) in the TGN and undergoes a process of activation that involves heterotrimeric GTP-binding protein subunits betagamma to regulate membrane fission. This fission reaction is used to generate transport carriers at the TGN that are en route to the cell surface. We now report that PKD is activated specifically by G protein subunit beta1gamma2 and beta3gamma2 via the Golgi apparatus-associated PKCeta. Compromising the kinase activity of PKCeta-inhibited protein transport from TGN to the cell surface. Expression of constitutively activated PKCeta caused Golgi fragmentation, which was inhibited by a kinase inactive form of PKD. Our findings reveal that betagamma, PKCeta, and PKD act in series to generate transport carriers from the TGN and their overactivation results in complete vesiculation of the Golgi apparatus. 相似文献
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