Abstract
By the method of IR spectroscopy it is established that the process of sorption of celiase, trypsin, chymotrypsin, streptase, plasminogen, and plasmin by monocarboxylcellulose (the content of COOH groups is 15 wt.%) is mainly identical. The determining role in the mechanism of binding of monocarboxylcellulose with the considered medicinal enzymes belongs to electrostatic interactions with the formation of ionic bonds between the COO− groups of the matrix and charged amine groups of protein molecules. It is established that the process of interaction of plasmin with oxidized cellulose takes a more active course than with other investigated enzymes. It is shown that the activity of interaction of the enzymes with monocarboxylcellulose can be evaluated by a change in the relative intensity of the band of stretching vibrations of C=O groups.
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