Biomedical subjects
Publications and source records attributed to V N Morozov.
The article presents experimental and clinical data on changes of homeostasis in frostbites. It is shown that the zone of injured tissues can be lessened by acting the mechanism of neurohumoral regulation with rausedyl, heparin and fibrinolysin.
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Hemostatic blood potential was studied in experiments on 400 rats, 25 dogs and in 120 patients, during changes of CNS reactivity after intraventricular injection of reserpine, adrenaline, and irritation of the thalamus ventromedial nucleus (VMN) or its destruction. CNS reactivity in dogs changed after intraarterial injections of acetylcholine, reserpine, heparin and fibrinolysin solutions. It was shown that activation of adrenergic structures of the hypothalamus by intraventricular adrenaline injections, or the hypothalamus VMN irritation, stimulated coagulation and depressed anticoagulation mechanisms of the blood, and increased hemostatic blood potential, that led to rejection of frostbitten tissues. Activation of the hypothalamus cholinergic structures by intraventricular injections of reserpine, destruction of the hypothalamus VMN, and intraarterial injections of acetylcholine, reserpine, heparin, fibrilysin and contrycal mixtures stimulated the blood anticoagulation mechanisms, decreased the hemostatic potential, led to retention of cryodestructed tissues.
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A method for taking stress-strain diagrams in microsamples prepared from glutaraldehyde-treated monocrystals and amorphous films of hen egg-white lysozyme has been developed. Analysis of the diagrams has shown that the deformation obeys Hooke's law within 0-2%. Upon further deformation of a crystalline sample (up to 6-10%), when a critical stress, sigma(cr), is reached, the protein molecules in the sample denature and become greatly extended. Depending on the crystal type and crystallographic direction, the sample length increases 2-4 times. The critical stress is essentially dependent on the factors affecting intra- and intermolecular interactions: temperature, hydration level and urea concentration. Mechanisms for mechanical denaturation are proposed.
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An analysis of the results of a combined psychophysiological examination has demonstrated that the absence of marked clinical manifestations cannot be considered as a valid criterion justifying the denial or discontinuation of inpatient treatment. Hence, the results of psychophysiological examination may serve only as an additional criterion in the evaluation of the patients' condition.
A preliminary analysis is presented of whether and to what extent thermal motion of protein molecules as rigid bodies contributes to the mobility found in X-ray and Mössbauer studies. A simple theory is advanced enabling the estimation of mean-square amplitudes of translational and librational motion of the protein molecules in crystals and amorphous glasses from the experimental data on the elastic properties of these solids. The values calculated and their dependence on the crystal packing, temperature and hydration level were found to be in good accord with the data of X-ray analysis and Mössbauer spectroscopy. The external modes were concluded to contribute significantly to the values of mean value of chi 2 measured by the last two methods meaning that the conventional amplitudes of internal motion in proteins were overestimated. The real average amplitude of thermal motion of atoms in the protein interior should be close to that in molecular crystals, in accordance with the crystal-like packing of atoms inside the protein globule and some other "crystal-like" physical characteristics such as Young's modulus, adiabatic compressibility and thermal expansion coefficient. Factors are discussed which determine the temperature dependence of the amplitudes of external and internal modes of protein motion.
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Cross-linked protein solids are proposed as new types of chemomechanical sensors for identification of biological molecules and measurement of their concentration. New sensors make use of the ability of proteins to specifically bind its ligands and to alter their conformation upon the binding. The use of immobilized proteins enables these conformational changes to be detected through the changes in mechanical properties of protein solid samples (stress, stain or the Young's modulus). Some advantages of the new sensors over enzyme probes are illustrated on considering the properties of papain sensor for alpha-N-benzoyl-L-arginine ethyl ester.
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Explore the source record for details and available documents.