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F Inoue

Publications and source records attributed to F Inoue.

At least 145 records · Page 8Linked to original sources

Use of spin label and the flow-induced ESR spectral difference for studying erythrocyte deformation.

ESR spin-labeling method is expanded to measure the macroscopic visco-elastic properties of erythrocytes. A suspension of erythrocytes with an incorporated fatty acid spin label was forced to flow through a flat ESR sample cells, and the ESR spectral change caused by the shear flow was utilized to assess the cell deformability. Chemical cross-linking or heat denaturation of membrane proteins to make the cells less deformable without any morphological change was found to reduce the relative spectral difference (delta h/h). This result indicates that the spectral difference is related to the cell deformation that accompanies the orientation of the cells in the shear flow. In addition, the average decay time (tau av) for the spectral difference observed when the flow was abruptly interrupted became shorter with an increase in the degree of cross-linking or heat-denaturation abruptly interrupted became shorter with an increase in the degree of cross-linking or heat-denaturation at 49 degrees C. Since the observed tau av is much shorter than the expected rotational correlation time for the erythrocyte, the decay is attributed to the deformation recovery process. It is demonstrated that the measurements of both delta h/h and tau av by ESR spectroscopy give qualitative information on the viscosity and the elasticity of the cell membrane system.

Blood Viscosity↗

Withdrawal akinesia.

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Basal Ganglia Diseases↗

Spin label study of erythrocyte deformability I. Electron spin resonance spectral change under shear flow.

A spin labeling method in electron spin resonance spectroscopy (ESR) is applied for the first time to study the deformability of human red blood cells (RBC). ESR measurements of a RBC suspension incubated with a fatty acid spin label were performed, using a narrow-gap flat ESR sample cell under various flow shear stresses (tau). Remarkable changes were observed in ESR spectra with tau, indicating that RBC are oriented in such a way that the greater part of the membrane surface is aligned parallel to the ESR cell walls. The diamide-treated, hardened RBC, in which the biconcave discoid shape remains intact under no shear stress, exhibit a smaller ESR spectral change with tau than the intact, demonstrating that the present method can be used to assess the deformation of RBC occurring with flow orientation. In particular, the relative amplitude of an ESR difference spectrum may be used as a measure of the elongation of RBC. The conclusion is further supported by experiments using glutaraldehyde-treated or heat-denatured RBC. All these ESR results are in good agreement with the corresponding results obtained by several different methods. The present spin labeling technique is thus proven to be applicable for evaluating RBC deformability.

Electron Spin Resonance Spectroscopy↗

Enhancing effect of clamping of the portal vein on the effectiveness of antitumor agents against lymph node metastasis.

An experimental study was made on the suppressive effect on lymph node metastasis of an antitumor agent administered during the clamping of the portal vein. When mitomyaneously clamped, a higher concentration of the drug was detected in the mesenteric lymph nodes compared to the conventional intravenous administration. The growth of mesenteric lymph node metastasis was markedly suppressed by the combined use of mitomycin-C and portal vein clamping. These results suggest that the procedure applied in the present study directs a high concentration of antitumor preparations to the lymph nodes in the portal vein region, and thus is a good method for the suppression of lymph node metastasis.

Animals↗

Electrophysiologic effects of propranolol on the human heart.

Effects of propranolol (10(-9) to 10(-4) Gm/ml) on various electrophysiologic properties of human papillary muscles obtained from patients undergoing corrective open heart surgery were studied to have an insight into the mechanism of its antiarrhythmic activity in man. Propranolol (10(-8) to 10(-6) Gm/ml) produced significant decreases in the action potential duration, effective refractory period and dv/dt of depolarization phase of action potential without significantly affecting the resting potential and amplitude of action potential. These effects were concentration dependent. High concentration (10(-4) Gm/ml) of propranolol not only produced greater decreases in the above parameters but also reduced the resting potential and amplitude of action potential. Although propranolol decreased both the action potential duration and effective refractory period, the shortening of the action potential duration was greater than the shortening of the effective refractory period. It shifted the membrane responsiveness curve to the right and down. It produced frequency dependent decreases in the dv/dt of phase 0 of action potential and the rate of repolarization. Propranolol also increased the threshold of stimulation. Propranolol produced electrophysiologic changes in the human myocardium qualitatively similar to those in canine myocardium. The probable mechanism of its antiarrhythmic activity in man has been discussed.

Action Potentials↗

Alpha-methyl derivatives of biogenic amines as inhibitors of monoamin oxidase.

The values of Km app and Vmax for three natural substrates of monoamine oxidase have been determined at various stages in the isolation of the enzyme from rat liver tissue. The results are consistent with the presence in the enzyme preparation of at least two distinct molecular forms of the enzyme. Using the alpha-methyl derivatives of the natural substrates as inhibitors of the enzyme, the substrate dependence of Ki further substantiates this view. In addition, the kinetics of the inhibition suggest that the value of Km app may not for all substrates, necessarily be a measure of the affinity of the substrate for the enzyme.

Amphetamines↗

Interaction of fibrinogen with detergent.

Both cationic and anionic detergents were found to precipitate fibrinogen by forming fibrinogen-detergent complexes. These complexes were soluble in distilled water, but the aqueous solutions were very unstable and the complexes precipitated in the presence of salt. In the interaction of fibrinogen with the cationic detergent, stearyltrimethyl-ammonium chloride, approximately 160 molecules of detergent were found to bind to one molecule of fibrinogen. In distilled water, the fibrinogen-stearyltrimethylammonium complex (FG-STA(Cl)) remained soluble in the presence of thrombin [ED 3.4.21.5] although the same peptides were released as those released from fibrinogen. Precipitation of FG-STA(Cl) by salt was found to be closely related to adsorption of the anion of the salt by the complex. Futher addition of salt resulted in solubilization of the precipitate, and the solubilization was also due to further adsorption of the anion onto the precipitate.

Animals↗

Purification of fibrinogen using cationic detergent.

Stearyltrimethylammonium chloride was used to isolate human fibrinogen, and purified protein was obtained by removing the detergent bound to it. Medium consisting of 0.015--0.03 mM fibrinogen-detergent complex, 0.85 M NaCl, 0.03 M sodium caprylate, and 30 per cent ethanol was found to be effective for renaturation of fibrinogen from the complex. The purified fibrinogen did not form any fibrils on incubation for 15 days with Ca-2+ at pH 7.2, and 37 degrees. The clottability of the purified fibrinogen was over 99 per cent. Immunochemical studies showed that the purified fibrinogen produced one precipitation line with a mixture of anti-human fibrinogen and anti-human serum. Although highly purified, the fibrinogen preparation still contained a trace of plasminogen.

Calcium↗

Chemical modification of carboxyl groups of fibrinogen and its effect on the binding of cationic detergent.

Carboxyl groups of native human fibrinogen were modified with glycine methyl ester and 1-ethyl-3(3-dimethylaminopropyl)carbodiimide. It seemed likely that the modification occurred stepwise. Approximately 26% of the carboxyl groups of fibrinogen was modified finally. The modified fibrinogen had no interaction with cationic detergent, and did not form any complex with the detergent. In dilute acid, fibrinogen was observed to show only a slight interaction with cationic detergent. It is probable that the exposed and ionized carboxyl groups are essential for the formation of a complex between fibrinogen and cationic detergent.

Carbodiimides↗