Physico-chemical and enzymatic properties of polymeric trypsin derivatives based on dextran
Lindenbaum, G.M.; Bogacheva, T.I.; Mirgorodskaia, O.A.; Moskvichev, B.V.; Tereshin, I.M.
Prikladnaia Biokhimiia i Mikrobiologiia 13(5): 685-691
1977
ISSN/ISBN: 0555-1099 PMID: 918022 Document Number: 110773
The molecular weight distribution, thermal stability during autolysis, resistance to human serum inhibitors as well as temperature optimum of native and dextran-modified trypsin were investigated. The seeming constants of autolytic inactivation and inhibition of native and modified trypsin were calculated. Trypsin polymer derivatives had higher molecular weight than the native enzyme. They also showed higher resistance to autolysis and serum inhibitors. Possible causes of the above effects are discussed.