Лечение тяжелых форм пневмоний

The paper presents data about the treatment of 223 patients with severe or extremely severe pneumonia, including 68 patients with a septic shock. The basic group (112 patients) was treated by plasmapheresis combined with cryoplasmatic-antifermentative therapy. The high efficacy of these methods in combination with the basic therapy for the elimination of the toxemia syndrome, inflammatory reaction and disseminated intravascular coagulation was demonstrated. The complex treatment reduces duration and severity of septic shock caused by pneumonia, accelerates the infiltration resolution and increases the survival rate for the patients with severe pneumonia.В работе приводятся данные о лечении 223 больных пневмониями тяжелого и крайнетяжелого течения, у 68 из которых наблюдался инфекционно-токсический шок. В программу лечения основной группы (112 пациентов) входили плазмаферез в сочетании с криоплазменно-антиферментной терапией. Показана высокая эффективность данной методики на фоне базисной терапии по устранению синдрома токсемии, воспалительной реакции, купированию ДВС-синдрома. Лечебный комплекс снижает длительность и тяжесть инфекционно-токсического шока при пневмонии, ускоряет ее разрешение, повышает выживаемость больных тяжелыми пневмониями

Characterization of a Three-Component Vanillate O-Demethylase from Moorella thermoacetica

The Moorella thermoacetica aromatic O-demethylase was characterized as an inducible three-component system with similarity to the methanogenic methanol, methylamine, and methanethiol methyltransferases and to the O-demethylase system from Acetobacterium dehalogenans. MtvB catalyzes methyl transfer from a phenylmethylether to the cobalt center of MtvC, a corrinoid protein. MtvA catalyzes transmethylation from MtvC to tetrahydrofolate, forming methyltetrahydrofolate. Cobalamin can substitute for MtvC

Crystallographic Snapshots of Cyanide- and Water-Bound C-Clusters from Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Nickel-containing carbon monoxide dehydrogenases (CODHs) reversibly catalyze the oxidation of carbon monoxide to carbon dioxide and are of vital importance in the global carbon cycle. The unusual catalytic CODH C-cluster has been crystallographically characterized as either a NiFe4S4 or a NiFe4S5 metal center, the latter containing a fifth, additional sulfide that bridges Ni and a unique Fe site. To determine whether this bridging sulfide is catalytically relevant and to further explore the mechanism of the C-cluster, we obtained crystal structures of the 310 kDa bifunctional CODH/acetyl-CoA synthase complex from Moorella thermoacetica bound both with a substrate H2O/OH− molecule and with a cyanide inhibitor. X-ray diffraction data were collected from native crystals and from identical crystals soaked in a solution containing potassium cyanide. In both structures, the substrate H2O/OH− molecule exhibits binding to the unique Fe site of the C-cluster. We also observe cyanide binding in a bent conformation to Ni of the C-cluster, adjacent the substrate H2O/OH− molecule. Importantly, the bridging sulfide is not present in either structure. As these forms of the C-cluster represent the coordination environment immediately before the reaction takes place, our findings do not support a fifth, bridging sulfide playing a catalytic role in the enzyme mechanism. The crystal structures presented here, along with recent structures of CODHs from other organisms, have led us toward a unified mechanism for CO oxidation by the C-cluster, the catalytic center of an environmentally important enzyme.United States. Dept. of Energy (Contract No. DE-AC02-05CH11231)United States. Dept. of Energy. Office of Basic Energy SciencesStanford Synchrotron Radiation Laborator

Transient B12-Dependent Methyltransferase Complexes Revealed by Small-Angle X-ray Scattering

In the Wood−Ljungdahl carbon fixation pathway, protein−protein interactions between methyltransferase (MeTr) and corrinoid iron−sulfur protein (CFeSP) are required for the transfer of a methyl group. While crystal structures have been determined for MeTr and CFeSP both free and in complex, solution structures have not been established. Here, we examine the transient interactions between MeTr and CFeSP in solution using anaerobic small-angle Xray scattering (SAXS) and present a global analysis approach for the deconvolution of heterogeneous mixtures formed by weakly interacting proteins. We further support this SAXS analysis with complementary results obtained by anaerobic isothermal titration calorimetry. Our results indicate that solution conditions affect the cooperativity with which CFeSP binds to MeTr, resulting in two distinct CFeSP/MeTr complexes with differing oligomeric compositions, both of which are active. One assembly resembles the CFeSP/MeTr complex observed crystallographically with 2:1 protein stoichiometry, while the other best fits a 1:1 CFeSP/MeTr arrangement. These results demonstrate the value of SAXS in uncovering the rich solution behavior of transient protein interactions visualized by crystallography.National Institutes of Health (U.S.) (NIH grant K99GM100008)National Institutes of Health (U.S.) (NIH grant F32GM090486)National Institutes of Health (U.S.) (NIH grant GM39451)National Institutes of Health (U.S.) (NIH grant GM69857)Howard Hughes Medical Institute (Investigator