Studies on the Amide and C-Terminal Residues in Proteins
نویسندگان
چکیده
Chibnall, A. C., Haselbach, C., Mangan, J. L. & Rees, M. W. (1958a). Biochem. J. 68, 122. Chibnall, A. C., Mangan, J. L. & Rees, M. W. (1958b). Biochem. J. 68, 111. Chibnall, A. C. & Rees, M. W. (1952). Biochem. J. 52, iW. Chibnall, A. C. & Rees, M. W. (1953). In The Chemical Structure of Proteins, p. 70. Ed. by Wolstenholme, G. E. W. & Cameron, M. P. London: J. and A. Churchill Ltd. Desnuelle, P. & Casal, A. (1948). Biochim. biophy8. Acta, 2, 64. Elliott, D. F. (1952). Biochem. J. 50, 542. Fraenkel-Conrat, H. L. & Olcott, H. S. (1945). J. biol. Chem. 161, 259. Mommaerts, W. F. H. M. & Neurath, H. (1950). J. biol. Chem. 185, 909. Moore, S. & Stein, W. H. (1954). J. biol. Chem. 211, 893. Peters, J. B. & Van Slyke, D. D. (1932). In Quantitative Clinical Chemi8try, vol. II, p. 385. London: Bailli6re, Tindall and Cox. Pregl, S. (1937). In Quantitative Organic Micro-analysis, 3rd ed., p. 171. London: J. and A. Churchill Ltd. Rees, M. W. (1946). Biochem. J. 40, 632.
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