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Foot-and-mouth disease virus (FMDV) is an important animal pathogen that belongs to the Aphthovirus genus of the Picornaviridae family and infects cattle and other cloven-hoofed animals. Seven serotypes (A, O, C, Asia1, SAT1, SAT2 and SAT3) have been identified serologically, and multiple subtypes occur within each serotype. FMDV enters cells by receptor-mediated endocytosis. By electron microscopy the FMD virion appears to be a round particle with a smooth surface and a diameter of about 25 nm. The FMD viral particle contains a positive-strand RNA genome of about 8500 nucleotides, enclosed within a protein capsid. The virus capsid is made up from 60 copies each of four virus-encoded proteins VP1 to VP4. The FMDV genome is composed of the 5’ non-translated region (5’NTR), the coding region, and the 3’ non-translated region (3’NTR). The genome encodes a single polyprotein, from which the different viral polypeptides are derived by viral proteases. FMDV populations are genetically and anti-genetically heterogeneous. FMDV have very high mutation rates.
The solubility of sodium coprecipitate in water and in salt solution of the composition corresponding to simulated milk ultrafiltrate was studied at 3000, 8000, 19000 and 110000 g. The molecular state of protein determining its solubility was defined together with the contribution of Ca, Mg, P, K and Na to the formation of this state. The (Ca+Mg)/(Na+K) weight ratio in the protein aggregates insoluble in the salt solution decreased with an increase in gravity. The constant (Ca+Mg)/N weight ratio and protein composition of the protein aggregates insoluble in the salt solution in the gravity ranging from 3000 to 110000 g suggested increased contributions of hydrophobic interactions and covalent bondings in the integration of protein particles as their size increased.
The paper reviews the molecular structure, distribution and the role of metabotropic glutamate receptors (mGluRs) as excitatory aminoacid receptors. These receptors comprise a family which consists of at least eight members (mGluR₁₋₈) and coupled to various intracellular second messenger systems through G-proteins. These receptors mediate the neuromodulatory action of glutamate, and have been traditionally divided into three main groups (mGluR I, II i III) based on sequence similarity. Recent progress in the development of specific antagonists (LY 367 385, MPEP for mGluR₁) and/or agonist LY 354740, ADPC for mGluR₂⁄₃ and L-AP4 for mGluR₄) for these receptors can significantly facilitate the prophilaxy and therapy of different types of pain.
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