Publications by authors named "E V Petrochenko"

FK506 binding proteins (FKBPs) catalyze the interconversion of cis-trans proline conformers in proteins. Importantly, FK506 drugs have anti-cancer and neuroprotective properties, but the effectors and mechanisms underpinning these properties are not well understood because the cellular function(s) of most FKBP proteins are unclear. FKBP25 is a nuclear prolyl isomerase that interacts directly with nucleic acids and is associated with several DNA/RNA binding proteins.

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Background: Generalized restricted blood flow is hallmark of CHF of any etiology, but the extent of microcirculation restriction and the role of intrinsic blood properties in heart failure remains unknown.

Objective: The aim of this study was to estimate the microvascular blood flow and hemorheological properties in chronic heart failure to test the hypothesis that CHF patients have altered peripheral blood flow which contributes to the tissue perfusion disturbances.

Methods: Cutaneous microvascular blood flow was estimated by Laser Doppler and Optical Tissue Oximetry techniques.

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Cancer progression is associated with activation of blood coagulation. Blood coagulation process, platelet hemostasis and hemorheological properties were evaluated in patients with solid tumors (n = 27) before and after surgery and in healthy control (n = 20). The main features of blood coagulation process in cancer patients were elevated intensity and shortened period of contact phase of coagulation and inhibited fibrinolysis stage.

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The reversed-phase HPLC of porcine insulin modified by fluorescent labeling with dansyl chloride, fluorescein isothiocyanate, and an N-hydroxysuccinimide ester of 3-carboxyl derivative of Nile Red was studied. Mono-, di-, and tri-Dns-insulins (substituted at residues Gly1 of the A-chain and Phe1 and Lys29 of the B-chain), as well as isomeric 5'- and 6'-fluorescein thiocarbamoyl-Phe1 insulin derivatives were separated on the analytical and semipreparative scale. The results were interpreted in terms of conservation of the globular structure in the modified proteins and their surface-mediated interaction with the reversed-phase sorbent.

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The membrane microsomal monooxygenase system can be reconstituted in solution from NADPH-specific flavoprotein and cytochrome P-450 which exist in the monomeric state in the presence of Emulgen 913 at molar ratio of the proteins and detergent of 1:1:300. Oxidized and dithionite-reduced monomers of cytochrome P-450 were much less thermostable than its initial aggregates, while thermal stability of NADPH-specific flavoprotein did not depend on its aggregation state. Binding spectra of cytochrome P-450 monomers with benzphetamine were atypical and had an absorbance minimum at 422 nm only.

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