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Isolation and characterization of five serine proteases with trypsin chymotrypsin and elastase like characteristics from the gut of the lugworm arenicola marina l. polychaeta


Journal of Comparative Physiology B Biochemical Systemic and Environmental Physiology 162(2): 159-167
Isolation and characterization of five serine proteases with trypsin chymotrypsin and elastase like characteristics from the gut of the lugworm arenicola marina l. polychaeta
Five proteases were isolated from the digestive fluid of the lugworm. Arenicola marina L. The enzymes (molecular weight 24.0-24.6 kDa) were classified as serine proteases. Three enzymes showed a cleavage specificity corresponding to mammalian trypsin (E.C. 3.4.21.4). One protease possessed a chymotrypsin-like cleavage pattern (EC. 3.4.21.1), and the fifth preferred cleavage behind short-chain amino acids like an elastase (E.C. 3.4.21.36). Detailed investigations revealed differences in molecular characteristics and cleavage patterns compared to mammalian proteases, especially in the chymotrypsin- and the elastase-like enzymes.


Accession: 007492413



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