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Clostridium perfringens substrate specificity

The n /b-a-D-2-acetamido-2-deoxygalactanase and a-D-2-acetamido-2-deoxy-galactosidase of Clostridium perfringens culture filtrates have been separated by polyacrylamide gel electrophoresis. The substrate specificities of the two enzymes were compared (see p. 387). [Pg.423]

X 10 ) and substrate specificities, and exhibited similar behaviour towards ions they differed slightly in pH optima, thermostabilities, and kinetic properties. The neuraminidases differ from Clostridium perfringens neuraminidase (mol. wt. 5.7 X 10 ) in substrate specificity, and were not inhibited by 4-chloro-mercuribenzoate. [Pg.353]

See other pages where Clostridium perfringens substrate specificity is mentioned: [Pg.325]    [Pg.122]    [Pg.134]    [Pg.196]    [Pg.266]    [Pg.348]    [Pg.134]    [Pg.361]    [Pg.335]    [Pg.118]    [Pg.148]    [Pg.509]    [Pg.395]    [Pg.424]    [Pg.363]    [Pg.36]    [Pg.271]    [Pg.274]    [Pg.295]    [Pg.302]   
See also in sourсe #XX -- [ Pg.305 ]



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