[The first episode of spontaneous pneumothorax (errors, hazards, complications)]. / Oshibki, opasnosti, oslozhneniia pri pervom épizode spontannogo pnevmotoraksa.

AIM: To analyze the errors and complications of surgical care in patients with the first episode of spontaneous pneumothorax at different hospitals. MATERIAL AND METHODS: From 2005 to 2015 three hundreds and seventeen patients with the first episode of spontaneous pneumothorax have been treated at the thoracic department of Volgograd State Medical University. Patients were divided into 2 groups: 79 of them underwent thoracotomy while in 238 cases minimally invasive technologies were applied. Faster preoperative management and earlier active surgical tactics were suggested. RESULTS: There were 6 the most typical violations of surgical care in 42% of patients with the first episode of spontaneous pneumothorax. Medical and diagnostic violations at regional centers and central district hospitals were the same, but there were differences in certain types of errors and their incidence. Minimally invasive technologies do not significantly affect the number of violations of thoracic surgery principles. Early procedures against the recurrence by using of thoracoscopic interventions reduce postoperative morbidity from 1.2 to 0.3% and mortality by 8.25 times.

Design of an artificial hemoprotein based on human serum albumin.

For modelling cytochrome P450-catalyzed reactions, an artificial hemoprotein was designed. Upon complex formation of human serum albumin with iron protoporphyrine IX, there occurred the incorporation of heme into the protein and formation of a specific complex with the albumin to heme molar ratio 2:1. The apparent dissociation constant Kd of the complex, as determined by optical absorption spectroscopic technique, was 1.9 +/- 0.4 M-6. Based on spectral studies and molecular modelling of the complex spatial structure, it was assumed that His 31 or His 90 may be the most probable 5th ligand for the heme iron. The artificial hemoprotein was able to catalyze (in the presence of riboflavin as electron carrier) the NADH-dependent aniline hydroxylation and dimethylaniline and amidopyrine N-demethylation. The electron transfer pathway from NADH to substrate was demonstrated. Flavin appears to serve as an input center (mediator) for the rapid transfer of electrons from NADH to heme, where substrate is oxidized. The same reactions were accomplished using riboflavin photoreduction in the hemoalbumin-riboflavin system with the unfocussed laser emission at lambda = 457.9 nm. As electron donor, metallic zinc was used. The artificial hemoprotein obtained was also able to catalyze H2O2-dependent oxidase reactions.

Comparative analysis of the secondary structural motifs of P450BM-3 and the regions located upstream of the calmodulin-binding domain in the nitric oxide synthases.

The proposed method of multiple alignment of secondary structures makes it possible to estimate the multidomain enzymes' structural similarity in those cases where, following alignment, the identity appears to be inadequate or too insignificant to estimate protein relationship in spite of their functional analogy. Multiple alignment of sequences, representing the secondary structural elements of the nitric oxide synthase (NOS) N-terminal "tails", localized upstream of the calmodulin (CAM)-binding domain, and the P450 superfamily representative P450BM-3 has revealed the existence of a common secondary structural motif, standing of 60% identity between the polypeptide chain packing of NOS and the full sequence of P450BM3. This fact may point to the existence of their common ancestor. Presence of the linker olygopeptides within NOS permitted us to determine the boundary of the cytochrome-like part of NOS.