ABSTRACT
An electrophoretic investigation of quantitative protein content in rat's' tissyes under chronic alcoholic intoxication has been done. It was shown the significant increase of protein content with molecular mass 55, 48-50, 43-45, 39-41 KDa and the decrease-of protein fractions with molecular mass 46-48, 34-35, 27-30, 16-18 KDa accordingly in liver and brain homogenates of experimental animals.
Subject(s)
Alcoholism/metabolism , Brain/drug effects , Ethanol/toxicity , Liver/drug effects , Nerve Tissue Proteins/metabolism , Alcoholism/physiopathology , Animals , Animals, Outbred Strains , Brain/metabolism , Brain Chemistry , Electrophoresis, Polyacrylamide Gel , Female , Liver/chemistry , Liver/metabolism , Molecular Weight , Nerve Tissue Proteins/isolation & purification , RatsABSTRACT
We studied the key parameters of the development of prediabetic state in rats maintained on a high-calorie diet. It was found that long-term feeding a high-calorie diet increased blood concentration of glucose, glycosylated hemoglobin, and insulin and reduced the rate of glucose uptake in comparison with rats receiving standard ration.
Subject(s)
Diet/adverse effects , Prediabetic State/etiology , Animals , Animals, Outbred Strains , Blood Glucose , Energy Intake , Female , Insulin Resistance , Prediabetic State/blood , RatsABSTRACT
Fibrinogen to fibrin conversion and then fibrin clot three-dimensional network formation is one of the final steps in the coagulation system activation. Different factors, such as the environment temperature and pH, ions, so on, render an effect on the fibrin gel formation. Recently, the presence or absences of interface between two phases influence on the fibrin gel structure during its formation have been shown. Studies of fibrin gel structure peculiarities formed at different conditions (between two phases and without one phase) are demonstrated in this article. The plasmin enzymatic hydrolysis of fibrin clots both with surface film and without it was investigated. Experimental data allow to make a conclusion that the fibrin clot structure changes depend on its essential influence on the plasmin hydrolysis process of these clots.
Subject(s)
Fibrin/chemistry , Thrombosis/metabolism , Electrophoresis, Polyacrylamide Gel , Fibrin/metabolism , Humans , Hydrolysis , Kinetics , Protein ConformationABSTRACT
Transformation of fibrinogen into fibrin with consequent formation of the fibrin clot trimeric structure is one of the final steps in the blood coagulation system. The plasminogen activation by the tissue plasminogen activator (t-PA) is one of the fibrinolysis system key reactions. The effect of different factors on transformation of plasminogen into plasmin is capable to change essentially the equilibrium between coagulation and fibrinolytic sections of haemostasis system. We have studied the plasminogen activation by tissue plasminogen activator on fibrin clots surface formed on the interface between two phases and in presence of one phase. The t-PA plasminogen activation rate on fibrin clots both with film and without it the latter has been analyzed. These data allow to assume that the changes of fibrin clot structure depend on its formations, as well as are capable to influence essentially on plasminogen activation process by means of its tissue activating agent.
