RESUMEN
The data on the completing level of a number of medical preparations on the basis of immobilized proteins, in particular, on the basis of enzymes are given. The firms and companies which successfully cooperate in the field of development of commercial programs for such preparations are listed. On the basis of own study a possibility to create some effective antitumor compounds in the next future is shown. The urgent and prospective application of the immobilized enzymes instead of the native ones in the medicine is grounded.
Asunto(s)
Enzimas Inmovilizadas , Antineoplásicos/administración & dosificación , Ensayos Clínicos como Asunto , Portadores de Fármacos , Interacciones Farmacológicas , Humanos , Ligandos , SolubilidadRESUMEN
L-asparaginase, covalently bound with water-soluble CM-cellulose, exhibited the elevated antileukemic activity in mice with inoculated lymphoid leukemia L5178y as compared with the native enzyme. The antileukemic activity of the immobilized enzyme was shown to depend on the content of the polymer bound with the enzyme; the polymer amount may be altered during the enzyme modification. The prolonged effect of immobilized L-asparaginase was observed in rabbit circulation.
Asunto(s)
Asparaginasa/uso terapéutico , Carboximetilcelulosa de Sodio , Enzimas Inmovilizadas/uso terapéutico , Metilcelulosa , Animales , Asparaginasa/sangre , Semivida , Leucemia L5178/tratamiento farmacológico , Metilcelulosa/análogos & derivados , Ratones , ConejosRESUMEN
Enzymatic and antileukemic effects of the complexes of L-asparaginase from E. coli and biologically active polymer dextran sulfate were studied to increase their therapeutic properties. The complex was characterized by more distinct substrate specificity, by an increase in the stability during storage, in thermostability as well as in the resistance to proteolysis. The increased antileukemic activity of the complex was observed in experimental lymphoid leukemia L5178y in mice. Use of the complex of L-asparaginase and dextran sulfate enabled to decrease distinctly the therapeutic dose of the enzyme.