ABSTRACT
We optimized the conditions of the covalent binding of bovine liver catalase to phosphate-cellulose matrices (gauze, granules, and paper with various surface density) and to acetate-cellulose porous membranes of different productivity. The capacity of the catalase binding to the molded cellulose carriers depends on the physico-chemical characteristics of the latter. The maximum concentration of the bound catalase after periodate oxidation of the carriers at room temperature was determined. The catalytic activity of the immobilized enzyme was quantified; under optimal conditions it is 24% for acetate-cellulose membranes and 24.3% for phosphate-cellulose paper and reduces with the increase of the total protein binding capacity of both the carriers.
Subject(s)
Catalase/metabolism , Cellulose/chemistry , Enzymes, Immobilized/metabolism , Animals , Catalysis , Cattle , Liver/enzymology , Oxidation-ReductionABSTRACT
The Institute of General and Inorganic Chemistry of the BSSR Academy of Sciences and the Byelorussian Research Institute of Blood Transfusion have developed and used in hospital practice a fundamentally new method of blood stabilization which does not require addition of alliens. Some part of calcium from blood plasma is extracted by filtrating the blood through layers of specially developed highly effective and biologically compatible fibrous sorbents of derivatives of cellulose (natural highpolymer). The blood may the used in all cases of homotransfusion and most expediently in extremely complicated cases, when direct blood transfusions are difficult. Stabilized blood may also be effectively used when large-quantity or exchange blood transfusions have to be quickly performed, to resuscitate patients from clinical death, to stop haemorrhage caused by disturbances in blood coagulation, to treat anaemia of different etiology, including radiation illness, and in case of sensitiveness to citrate solutions (serious affections of kidneys, liver and heart).
