[Study of the structural organization of OSCP--subunits of H+-ATPase of porcine heart mitochondria]. / Issledovanie strukturnoi organizatsii OSCP--sub''edinitsy H+-ATP-azy mitokhondrii serdtsa svin'i.

Unmodified and citraconilated OSCP of the pig heart mitochondrial H(+)-ATPase were hydrolysed by proteinase from Staphylococcus aureus V8 and trypsin, respectively. To purify the individual peptides, various types of HPLC and covalent chromatography on SH-Sepharose were used. By the automatic Edman method complete or partial amino acid sequences of the peptides obtained were determined, thus allowing for the reconstruction of the primary structure of pig OSCP. A linear antigenic determinant recognizable by A1 monoclonal antibody against bovine OSCP, was localized. Studies showed Gly43 residue (bovine OSCP) to be replaced by Ala43 (pig OSCP), which is responsible for a decrease of the affinity of the monoclonal antibody A1 to pig OSCP. Comparative analysis of primary structures of bovine and pig OSCP was carried out.

[Leukocyte transfusions in the treatment of sepsis]. / Leikotransfuzii v lechenii sepsisa.

Leukotransfusion from ordinary donors and those immunized by staphylococcal anatoxin were used in complex treatment of 55 patients in a catabolic phase of different forms of sepsis. It was found that transfusion of leukosuspensions, immune ones in particular, had pronounced immunostimulating, detoxicating, antibacterial and anti-inflammatory effects. A short course of transfusions of allogenic leukocytes can be fulfilled without a selection by the HLA system.

[Primary structure of the OSCP-protein, conferring the oligomycin sensitivity to the H+-ATPase complex. II. Hydrolysis of OSCP with proteinase from Staphylococcus aureus and reconstruction of the polypeptide chain]. / Pervichnaia struktura OSCP-belka, pridaiushchego mitokhondrial'nomu H+-ATP-aznomu kompleksu chuvstvitel'nost' k oligomitsinu. II. Gidroliz OSCP proteinazoi iz Staphylococcus aureus i rekonstruktsiia polipeptidnoi tsepi belka.

Hydrolysis of OSCP of bovine heart mitochondria by proteinase from Staphylococcus aureus V8 was followed by isolation of all individual peptides by means of gel-filtration and HPLC. Structural analysis of the peptides allowed to arrange BrCN-fragments and to reconstruct the complete amino acid sequence of the protein. Comparative structural analysis revealed existence of a certain homology between OSCP and delta- and b-subunits of the E. coli H+-ATPase, which are necessary for interaction of catalytic and proton-conducting parts of the bacterial enzyme.