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1.
Farmakol Toksikol ; 44(3): 322-6, 1981.
Article in Russian | MEDLINE | ID: mdl-6456930

ABSTRACT

The cholecystographic radiopaque agents, adipiodon and endographin, unlike the urographic contrast agents, triombrin and iodamide, decrease the fluorescence intensity of hydrophobic probes 1-anilinonaphthalene-8-sulfonate and 4-dimethylaminochalcone in plasmic membranes (PM) of rat hepatocytes primarily at the expense of the lowering of the constant of probe association with the membranes. The similar but less marked effects were discovered in experiments with lecithin lyposomal preparations. As regards the intensity of action, cardiotrast and triotrast an intermediate position between the two groups of radiographic contrast agents. Adipiodon and endographin induce an inhibition of membranous Mg+2 (Na+, K+) ATPase, which correlates with their effect on the structure of the hepatocyte PM. The data obtained allow a conclusion that, unlike the urographic agents, the cholecystographic radiopaque agents are bound to the definite areas of the hepatocytic PM and provoke alterations in the activity of membranous APTase because of the conformational rearrangements of the membranes.


Subject(s)
Cell Membrane/drug effects , Contrast Media/pharmacology , Liver/drug effects , Acetrizoic Acid/pharmacology , Adenosine Triphosphatases/metabolism , Animals , Diatrizoate Meglumine/pharmacology , Female , Fluorescent Dyes/metabolism , Iodamide/pharmacology , Iodipamide/pharmacology , Iodopyracet/pharmacology , Liposomes , Male , Rats
2.
Farmakol Toksikol ; 40(4): 445-7, 1977.
Article in Russian | MEDLINE | ID: mdl-20329

ABSTRACT

The effect of roentgen-contrast media on the activity of the NADP'N and NAD'N-dependent electron-transport chains of the rats liver microsomes was studied. Bilignost, cardiotrast, triiotrast and triombrin are shown to lower the rate of the NADP'N oxidation by the rats' liver microsomes and have no effect (except for triiotrast) upon the rate of the NAD'N oxidation. It is presumed that the relative resistance of the NAD'N-specific flavoproteid is due to the presence of a hydrophobic layer impervious to the polar molecules of the contrast media.


Subject(s)
Contrast Media/pharmacology , Microsomes, Liver/metabolism , NADP/metabolism , NAD/metabolism , Acetrizoic Acid/pharmacology , Animals , Diatrizoate/pharmacology , Iodipamide/pharmacology , Iodopyracet/pharmacology , Male , Microsomes, Liver/drug effects , Oxidation-Reduction , Rats
3.
Invest Radiol ; 11(4): 303-8, 1976.
Article in English | MEDLINE | ID: mdl-955839

ABSTRACT

Evidence is presented for the activation of serum complement by contrast media, in vitro and in vivo. Activation as a function of concentration was measured and the increasing order of effectiveness was found to be metrizamide, iothalamate, diatrizoate, acetrizoate, iodipamide and iopanoate. This order is the same as for protein binding and enzyme inhibition. The activation mechanism for iodipamide, and by inference for the other compounds, does not involve gamma-globulin aggregation. Serial daily injections in normal dogs resulted in substantial declines in serum complement over several days. Guinea pigs which were depleted of serum complement with cobra venom factor were found to be no less sensitive to lethal doses of iodipamide than those with normal complement. Implications of these findings are discussed.


Subject(s)
Complement System Proteins , Contrast Media/pharmacology , Acetrizoic Acid/pharmacology , Animals , Complement Inactivator Proteins , Diatrizoate/pharmacology , Dogs , Enzyme Inhibitors/pharmacology , Female , Guinea Pigs , Humans , In Vitro Techniques , Iodipamide/pharmacology , Iopanoic Acid/pharmacology , Iothalamic Acid/pharmacology , Male , Metrizamide/pharmacology , Protein Binding , Snake Venoms
4.
Farmakol Toksikol ; 39(4): 444-8, 1976.
Article in Russian | MEDLINE | ID: mdl-1027570

ABSTRACT

Structural changes in the human serumal albumin under the effect of roentgen-contrast media, viz. bilignost, triiotrast, endografine, iodamide, triombrine and cardiotrast, were investigated by the method of fluorescence. The complex-formation of albumin with triiodotrast, bilignost and endografine was shown to call forth a short-wave shift of the fluorescence peak by approximately 20 nm. The binding section for these substances is characterized by an association constant equalling 1.2-10(5) M-1. The authors presume that triiodotrast, bilignost and endografine cause changes in the microstructure of the aqueo-protein layer in the area of the tryptophan residue localization. As to triombine, iodamide and cardiotrast fluorescence failed to disclose their combination with the human serumal albumin.


Subject(s)
Contrast Media/pharmacology , Serum Albumin/pharmacology , Acetrizoic Acid/pharmacology , Diatrizoate/pharmacology , Drug Interactions , Humans , Iodamide/pharmacology , Iodipamide/pharmacology , Iodopyracet/pharmacology , Protein Binding , Serum Albumin/analysis , Spectrometry, Fluorescence
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