Abstract
THE work of Miwa and co-workers1,2 showed that the relative specificity of β-glucosidase, expressed in terms of the ratio of enzyme activity toward β-glucosides with different aglucons, differs over a wide range depending on the source of the enzyme preparations. These differences are considered to be due to the difference in the structure of enzyme proteins themselves rather than contaminating substances, since they remain almost unchanged upon fractionation of enzyme preparations as well as with preparations of different purity.
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References
Miwa, T., Cheng, C., Fujisaki, M., and Toishi, A., Acta Phytochim., Japan, 10, 155 (1937).
Miwa, T., Cheng, C., Miwa, A., Fujisaki, M., and Outi, K., Sci. Rep. Tokyo Bunrika Daig., Sec. B, 6, 11 (1942).
Niwa, K., J. Biochem., Japan, 37, 301 (1950).
Herriott, R. M., “Advances in Protein Chem.”, 3, 170 (1947).
Helferich, B., and Winkler, S., Z. physiol. Chem., 221, 98 (1937).
Miwa, T., et al. (published data in Japanese).
Pigman, W. W., “Advances in Enzymol.”, 4, 41 (1946).
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MURAKAMI, Y. Relative Specificity of the Chemically Modified ‘Asperglllus niger β-Glucosidase’. Nature 171, 522–523 (1953). https://doi.org/10.1038/171522a0
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DOI: https://doi.org/10.1038/171522a0
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