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- W2030605090 abstract "Biotechnology and BioengineeringVolume 21, Issue 12 p. 2359-2363 Communications to the EditorFree Access Nonporous magnetic supports for proteases, cell-lytic enzymes, and ribonuclease: Limits of reactant size P. J. Halling, P. J. Halling Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, EnglandSearch for more papers by this authorJ. A. Asenjo, J. A. Asenjo Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, EnglandSearch for more papers by this authorP. Dunnill, P. Dunnill Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, EnglandSearch for more papers by this author P. J. Halling, P. J. Halling Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, EnglandSearch for more papers by this authorJ. A. Asenjo, J. A. Asenjo Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, EnglandSearch for more papers by this authorP. Dunnill, P. Dunnill Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, EnglandSearch for more papers by this author First published: December 1979 https://doi.org/10.1002/bit.260211217Citations: 14AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 G. J. H. Melrose, Rev. Pure Appt. Chem., 83 (1971). 2 P. A. Munro, M. D. Lilly, and P. Dunnill, Biotechnol. Bioeng., 19, 101 (1977). 3 G. H. Fleet and H. J. Phaff, J. Bacteriol., 119, 207 (1974). 4 P. J. Hetherington, M. Follows, P. Dunnill, and M. D. Lilly, Trans. Inst. Chem. Eng., 49, 142 (1971) 5 P. J. Halling and P. Dunnill, Biotechnol. Bioeng., 21, 393 (1979). 6 W. Rick, in Methods of Enzymatic Analysis, H. U. Bergmeyer, Ed. (Springer Verlag, Berlin, 1963), p. 807. 7 K. A. Walsh and P. E. Wilcox, in Methods of Enzymology, G. E. Perlmann and L. Lorand, Eds. (Academic, London, 1970), Vol. 19, p. 31. 8 K. Takahashi, J. Biochem. (Tokyo), 49, 1 (1961). 9 F. W. Ballardie and B. Capon, Chem. Commun., 828 (1972). 10 R. C. Davies, A. Neuberger, and B. M. Wilson, Biochim. Biophys. Acta, 178, 294 (1969). 11 J. S. O. Bacon, A. H. Gordon, D. Jones, I. F. Taylor, and D. M. Webley, Biochem. J., 120, 67 (1970). 12 N. Nelson, J. Biol. Chem., 153, 375 (1944). 13 J. A. Ansenjo, PhD thesis, University of London, 1978. 14 P. J. Halling and P. Dunnill, Biotechnol. Bioeng., 21, 2365 (1979). 15 P. J. Halling and P. Dunnill, submitted for publication. Citing Literature Volume21, Issue12December 1979Pages 2359-2363 ReferencesRelatedInformation" @default.
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