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The behavior of extramitochondrial protein synthesis and of mitochondrial RNA and protein synthesis was examined in the cytoplasts of African green monkey kidney cells (TC-7 subline) at different times following enucleation by cytochalasin B. The rate of incorporation of [3H]isoleucine into protein of the soluble cytoplasmic fraction decreased in an approximately exponential fashion, with a half-life of about five hours, during the first 26 hours after enucleation. Discrete mitochondrial 16 S, 12 S and 4 S RNA components were identified among the products of cytoplast RNA synthesis. The rates of [3H]uridine incorporation into the 16 and 12 S RNA components as well as into total RNA declined progressively after enucleation to a barely detectable level by the 20th hour. By contrast, the rate of chloramphenicol-sensitive [3H]isoleucine incorporation into protein (due to mitochondrial protein synthesis) did not undergo a substantial decline for at least 20 hours in TC-7 cytoplasts; instead, a reproducible transient stimulation occurred in the first hours following enucleation. The products of mitochondrial protein synthesis pulse-labeled in nucleated cells and in cytoplasts 24 hours after enucleation exhibited similar electrophoretic profiles. 相似文献
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Gary Parkinson Simon Gaisford Qian Ru Alastair Lockwood Ashkan Khalili Rose Sheridan Peng T. Khaw Steve Brocchini Hala M. Fadda 《AAPS PharmSciTech》2012,13(4):1063-1072
We are developing tablet dosage forms for implantation directly into the subconjunctival space of the eye. The matrix metalloproteinase inhibitor, ilomastat, has previously been shown to be efficacious at suppressing scarring following glaucoma filtration surgery (GFS). We report on the physical characterisation of ilomastat which is being developed for ocular implantation. Since ilomastat is being considered for implantation it is necessary to examine its polymorphs and their influence on aspects of the in vitro drug release profile. X-ray powder diffraction identified two polymorphs of ilomastat from different commercial batches of the compound. Tablets were prepared from the two different polymorphs. Isothermal perfusion calorimetry was used to show that amorphous content is not increased during tablet formulation. The melting points of the two polymorphs are 188 and 208°C as determined by differential scanning calorimetry. Utilising single crystal X-ray diffraction, the structural conformations and packing arrangements of the different polymorphs were determined. The orthorhombic crystal crystallised as a monohydrate while the second monoclinic crystal form is non-solvated. Ilomastat tablets prepared from the two different solid forms exhibited similar drug release profiles in vitro under conditions mimicking the aqueous composition, volume and flow of the subconjunctival space after GFS. This suggests that a reproducible dose at each time point during release after implantation should be achievable in vivo with ilomastat tablets prepared from the two polymorphs identified. 相似文献
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Acute oral administration of ethanol (3.2g/kg) to normal rats increased DOPAC levels and DOPA formation in the caudate nucleus but had no effect in the substantia nigra and frontal cortex and failed to modify dopamine (DA) levels in any of the above brain areas. Complete tolerance to the stimulant effect on DOPA formation developed after chronic ethanol administration (3.2g daily for 60 days). In chronically treated rats, 24 hrs after ethanol withdrawal, DA levels in the frontal cortex were 60% higher than in controls and were unchanged in the substantia nigra and caudate nucleus as were DOPAC levels in all areas studied. At this time, the administration of ethanol caused a long-lasting depletion of DA and a parallel increase of DOPAC levels in all areas analyzed. The results indicate that acute and chronic ethanol release DA stores but, in the acute condition, DA depletion is prevented by increased synthesis. 相似文献
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Nina Franko Konstantinos Grammatoglou Gabriele Costantino Aigars Jirgensons Andrea Mozzarelli 《Journal of enzyme inhibition and medicinal chemistry》2018,33(1):1343-1351
O-acetylserine sulfhydrylase (OASS) is the pyridoxal 5′-phosphate dependent enzyme that catalyses the formation of L-cysteine in bacteria and plants. Its inactivation is pursued as a strategy for the identification of novel antibiotics that, targeting dispensable proteins, holds a great promise for circumventing resistance development. In the present study, we have investigated the reactivity of Salmonella enterica serovar Typhimurium OASS-A and OASS-B isozymes with fluoroalanine derivatives. Monofluoroalanine reacts with OASS-A and OASS-B forming either a stable or a metastable α-aminoacrylate Schiff’s base, respectively, as proved by spectral changes. This finding indicates that monofluoroalanine is a substrate analogue, as previously found for other beta-halogenalanine derivatives. Trifluoroalanine caused different and time-dependent absorbance and fluorescence spectral changes for the two isozymes and is associated with irreversible inhibition. The time course of enzyme inactivation was found to be characterised by a biphasic behaviour. Partially distinct inactivation mechanisms for OASS-A and OASS-B are proposed. 相似文献
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Roberto Mattioli Marco Biancucci Amira El Shall Luciana Mosca Paolo Costantino Dietmar Funck Maurizio Trovato 《BMC plant biology》2018,18(1):356