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29 results on '"Orlov, V. N."'

18. METHOD OF SUPPRESSING FALSE SIGNALS (SPOSOB PODAVLENIYA LOZHNYKH SIGNALOV)

Author

FOREIGN TECHNOLOGY DIV WRIGHT-PATTERSON AFB OHIO, Sokolinskii,A. G., Orlov,V. N., FOREIGN TECHNOLOGY DIV WRIGHT-PATTERSON AFB OHIO, Sokolinskii,A. G., and Orlov,V. N.

Abstract

The patent describes a method of false-signal suppression in ultrasonic delay lines with multiple signal reflection in a rectangular acoustic line containing reflecting platforms. To equalize false signals at the output of lines, part of reflecting platforms is offset in parallel to the other in the plane of the beam direction., Edited trans. of Patent (USSR) 177 458, 27 Aug 64, by E. Harter.

Published
1967

19. PROCEEDINGS OF THE GROUP SCIENTIFIC AND TECHNICAL CONFERENCE ON PROBLEMS OF FLUID MECHANICS (SELECTED PARTS)

Author

FOREIGN TECHNOLOGY DIV WRIGHT-PATTERSON AFB OHIO, Orlov,V. N., Freidin,A. S., Gorelov,G. M., Lyakhov,V. K., Temnikov,A. V., FOREIGN TECHNOLOGY DIV WRIGHT-PATTERSON AFB OHIO, Orlov,V. N., Freidin,A. S., Gorelov,G. M., Lyakhov,V. K., and Temnikov,A. V.

Abstract

Table of Contents: Experimental determination of heat exchange intensification in a biangular channel with local expansion of the conduit cross section, Some results of an analysis of experimental data on the intensification of heat emission in channels, The calculation of thermal characteristics of heat exchange devices, Some results of wind tunnel tests of plane diffuser cascades with low rates of flow, Results from an experimental investigation of a diffuser with additional flow pressure at the outlet, Coefficients of heat transfer and hydraulic resistance as functions of longitudinal and transverse nonisothermicity in turbulent motion of fluid under internal-problem conditions, Application of electrothermal analogy to study of heat transfer in streamlined bodies of arbitrary shape., Doklady Kustovoi Nauchno Tekhnicheskoi Konferentsii Po Voprosam Medhaniki Zhidkosti i Gasa, Unedited rough draft trans. Aviatsionnyi Institut, Kuybyshev. Trudy (USSR) v15 (sic) p106-56, 299-307 1963.

Published
1966

24. [Hemorrhage in Dieulafoy disease as an example of an acute gastro-intestinal bleeding of uncertain etiology].

Author

Trotsenko SN, Orlov VN, and Damydiuk AP

Subjects
Acute Disease, Aged, 80 and over, Duodenal Diseases diagnosis, Duodenum blood supply, Electrocoagulation, Endoscopy, Digestive System, Gastrointestinal Hemorrhage diagnosis, Humans, Male, Treatment Outcome, Duodenal Diseases surgery, Duodenum surgery, Gastrointestinal Hemorrhage etiology, Gastrointestinal Hemorrhage surgery
Published
2010

25. [Dangers of diabetic pseudoperitonitis in practice of surgeon].

Author

Orlov VN, Trotsenko SN, and Podroĭko IuI

Subjects
Adult, Critical Care methods, Diabetes Mellitus, Type 1 therapy, Diabetic Ketoacidosis therapy, Diagnosis, Differential, Humans, Laparoscopy, Male, Peritonitis therapy, Treatment Outcome, Young Adult, Diabetes Mellitus, Type 1 diagnosis, Diabetes Mellitus, Type 1 surgery, Diabetic Ketoacidosis diagnosis, Diabetic Ketoacidosis surgery, Peritonitis diagnosis, Peritonitis surgery
Published
2010

27. [An acute gastric dilatation complicated by necrosis].

Author

Orlov VN, Koveshnikov AV, Podroĭko IuI, and Trotsenko SN

Subjects
Acute Disease, Anastomosis, Roux-en-Y, Gastrectomy, Gastric Dilatation diagnostic imaging, Humans, Male, Middle Aged, Necrosis, Stomach diagnostic imaging, Stomach surgery, Treatment Outcome, Ultrasonography, Gastric Dilatation pathology, Gastric Dilatation surgery, Stomach pathology
Published
2009

28. Changes in the thermal unfolding of p-phenylenedimaleimide-modified myosin subfragment 1 induced by its 'weak' binding to F-actin.

Author

Kaspieva OV, Nikolaeva OP, Orlov VN, Ponomarev MA, Drachev VA, and Levitsky DI

Subjects
Animals, Calorimetry, Differential Scanning, Cross-Linking Reagents, Electrophoresis, Polyacrylamide Gel, Maleimides metabolism, Myosin Subfragments metabolism, Protein Binding, Protein Folding, Rabbits, Temperature, Actins metabolism, Maleimides chemistry, Myosin Subfragments chemistry
Abstract

Differential scanning calorimetry (DSC) was used to analyze the thermal unfolding of myosin subfragment 1 (S1) with the SH1 (Cys-707) and SH2 (Cys-697) groups cross-linked by N,N'-p-phenylenedimaleimide (pPDM-S1). It has been shown that F-actin affects the thermal unfolding of pPDM-S1 only at very low ionic strength, when some part of pPDM-S1 binds weakly to F-actin, but not at higher ionic strength (200 mM KCl). The weak binding of pPDM-S1 to F-actin shifted the thermal transition of pPDM-S1 by about 5 degrees C to a higher temperature. This actin-induced increase in thermal stability of pPDM-S1 was similar to that observed with 'strong' binding of unmodified S1 to F-actin. Our results show that actin-induced structural changes revealed by DSC in the myosin head occur not only upon strong binding but also on weak binding of the head to F-actin, thus suggesting that these changes may occur before the power-stroke and play an important role in the motor function of the head.

Published
2001
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29. Complexes of smooth muscle tropomyosin with F-actin studied by differential scanning calorimetry.

Author

Levitsky DI, Rostkova EV, Orlov VN, Nikolaeva OP, Moiseeva LN, Teplova MV, and Gusev NB

Subjects
Animals, Calorimetry, Differential Scanning, Dimerization, Ducks, Gizzard, Avian, Hot Temperature, Nephelometry and Turbidimetry, Phalloidine pharmacology, Protein Binding, Protein Folding, Protein Multimerization, Rabbits, Actins metabolism, Muscle, Smooth metabolism, Tropomyosin metabolism
Abstract

Differential scanning calorimetry (DSC) and light scattering were used to analyze the interaction of duck gizzard tropomyosin (tropomyosin) with rabbit skeletal-muscle F-actin. In the absence of F-actin, tropomyosin, represented mainly by heterodimers, unfolds at 41 degrees C with a sharp thermal transition. Interaction of tropomyosin heterodimers with F-actin causes a 2-6 degrees C shift in the tropomyosin thermal transition to higher temperature, depending on the tropomyosin/actin molar ratio and protein concentration. A pronounced shift of the tropomyosin thermal transition was observed only for tropomyosin heterodimers, and not for homodimers. The most pronounced effect was observed after complete saturation of F-actin with tropomyosin molecules, at tropomyosin/actin molar ratios > 1 : 7. Under these conditions, two well-separated peaks of tropomyosin were observed on the thermogram besides the peak of F-actin, the peak characteristic of free tropomyosin heterodimer, and the peak with a maximum at 45-47 degrees C corresponding to tropomyosin bound to F-actin. By measuring the temperature-dependence of light scattering, we found that thermal unfolding of tropomyosin is accompanied by its dissociation from F-actin. Thermal unfolding of tropomyosin is almost completely reversible, whereas F-actin denatures irreversibly. The addition of tropomyosin has no effect on thermal unfolding of F-actin, which denatures with a maximum at 64 degrees C in the absence and at 78 degrees C in the presence of a twofold molar excess of phalloidin. After the F-actin-tropomyosin complex had been heated to 90 degrees C and then cooled (i.e. after complete irreversible denaturation of F-actin), only the peak characteristic of free tropomyosin was observed on the thermogram during reheating, whereas the thermal transitions of F-actin and actin-bound tropomyosin completely disappeared. Therefore, the DSC method allows changes in thermal unfolding of tropomyosin resulting from its interaction with F-actin to be probed very precisely.

Published
2000
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