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Isolation and partial characterization of a protease from Cucurbita ficifolia
Author(s) -
Curotto Emilia,
González Gustavo,
O'Reilly Sybil,
Tapia Guillermina
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80162-0
Subject(s) - iodoacetic acid , protease , alkaline protease , enzyme , biochemistry , isolation (microbiology) , cucurbita , substrate (aquarium) , molecular mass , chemistry , chromatography , biology , microbiology and biotechnology , ecology
A protease from the pulp of Cucurbita ficifolia was purified. Its molecular mass was estimated to be about 60 kDa. Its maximum activity is in the alkaline region against azocollagen as substrate. The enzyme is inhibited by phenylmethylsulphonyl fluoride but not by EDTA and iodoacetic acid.