[Low-density lipoprotein heterocomplexes].
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Biomedical subjects
Publications and source records attributed to Z Skrzydlewski.
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Native LDL are degraded by the protease of the lysosomal extract but they are not sensitive to isolated cathepsin D. Protamine increases the sensitivity of LDL to the effect of lysosomal protease and makes them sensitive to the effect of cathepsin D. Degradation of LDL by lysosomal protease is most intensive between pH 4.0 and 4.5 but in case of LDL bound with protamine it is most intensive at pH 4.5--5.0.
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By means of chemical methods and immunodiffusion technique it has been shown that low density lipoproteins incorporate into the structure of fibrin clot formed both in purified systems and in the blood plasma. Quantity of the incorporated lipoproteins into the fibrin depends on the concentration of fibrinogen and low density lipoproteins in the blood plasma. Rinsing of the fibrin with solutions of chemical compounds destroying different types of binding show that low density lipoproteins couple with the fibrin clot by means of ion and hydrogen bindings.
Low-density lopoproteins (LDL) form soluble and insoluble complexes with the total histone and its fractions. The bulk of these complexes is formed by the arginine-rich histone fraction. LDL are bound with histones by means of ion binding.
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Intravenous administration of histones or protamine to dogs resulted in a fall of the number of blood platelets, a lowered prothrombin consumption, a fall in the fibrinogen level, activation of the fibrinolytic system and deterioration of blood clot retraction.