Abstract
THE general attributes of ficin and its enzymic action have not been thoroughly described in the literature. The work of Winnick et al. 1 showed conclusively that ficin was a sulphydryl enzyme. More recently the kinetics of ficin on arginine derivatives have been studied2. In the present communication its electrophoretic and ultracentrifugal behaviour are described. The optimal conditions for activity and stability were also established. In further characterization of its properties, the effect of acetylation of its free arnino-groups on the activity and stability was studied.
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References
Winnick, T., Cone, W. H., and Greenberg, D. M., J. Biol. Chem., 153, 465 (1944).
Bernhard, S. A., and Gutfreund, H., Biochem. J., 63, 61 (1956).
Olcott, H. S., and Fraenkel-Conrat, H., Chem. Rev., 41, 151 (1947).
Cohen, Wm., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 67, 479 (1957).
Cohen, Wm., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 76, 204 (1958).
Terminiello, L., Sri Ram, J., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 57, 252 (1955).
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COHEN, W. Characterization of Ficin. Nature 182, 659–660 (1958). https://doi.org/10.1038/182659a0
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DOI: https://doi.org/10.1038/182659a0
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