N.N. Burdenko Voronezh State Medical University
Voronezh, Voronezh, Russian Federation
Sevastopol State University
Voronezh, Voronezh, Russian Federation
The composition and location of charged and hydrophobic amino acid residues of trypsin from Bos taurus and collagenase from Clostridium histolyticum were studied. The percentage ratio of different types of amino acids on the surface of enzymes was determined. It was established that charged and hydrophobic amino acid residues are distributed unevenly on the surface of the molecules, forming sections of a local cluster. It has been suggested that the most promising carriers for the immobilization of the proteases we studied are hydrophobic polymeric materials, which are likely to interact with one of the sites on the surface of enzyme molecules.
trypsin from Bostaurus, collagenase from Clostridium histolyticum, binding sites, charged amino acid residues, hydrophobic amino acid residues
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