Abstract
ALTHOUGH proteolytic activity has been shown by Berridge1 in a partially crystalline preparation of rennin, and by De Baun, Connors and Sullivan2 in a preparation 75 per cent pure, there has hitherto been no published proof that the activity is not due to contamination. Moreover, it has been implied that rennin has only weak proteolytic activity3.
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References
Berridge, N. J., Biochem. J., 39, 179 (1945).
De Baun, R. M., Connors, W. M., and Sullivan, R. A., Arch. Biochem. and Biophys., 43, 324 (1953).
Nitschmann, H., and Varin, R., Helv. Chim. Acta, 34, 1421 (1951).
Berridge, N. J., and Woodward, C., Biochem. J., 54, xix (1953).
Northrop, Kunitz, and Herriott, “Crystalline Enzymes” (Columbia Univ. Press, 1948).
Ryle, A. P., Sanger, F., Smith, L. F., and Kitai, Ruth, Biochem. J., 60, 541 (1955).
Holter and Li, S.-O., Acta Chem. Scand., 4, 1321 (1950).
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FISH, J. Activity and Specificity of Rennin. Nature 180, 345 (1957). https://doi.org/10.1038/180345a0
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DOI: https://doi.org/10.1038/180345a0
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