Abstract
Comparison of the amino-acid sequences of the three proteins shows that a common pattern of invariant non-polar residues exists. This permits a tentative assignment of exterior and interior positions. Glutamic acid at position 188 looks like the ionic binding site for trypsin substrates.
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References
Hartley, B. S., Brown, J. R., Kauffman, D. L., and Smillie, L. B., Nature, 207, 1157 (1965).
Walsh, K. A., and Neurath, H., Proc. US Nat. Acad. Sci., 52, 884 (1964).
Mikeš, O., Holeyšovský, Tomášek, V., and Šorm, F., Biochem. Biophys. Res. Commun., 24, 346 (1966).
Keller, P. J., Cohen, E., and Neurath, H., J. Biol. Chem., 233, 344 (1958).
Guy, O., Gratecos, D., Rovery, M., and Desnuelles, P., Biochim. Biophys. Acta, 115, 404 (1966).
Smillie, L. B., Enenkel, A. G., and Kay, C. M., J. Biol. Chem., 241, 2097 (1966).
Kassell, B., and Laskowski, M., J. Biol. Chem., 236, 1996 (1962).
Smillie, L. B., and Hartley, B. S., Biochem. J., 105, 1125 (1967).
Enenkel, A. G., and Smillie, L. B., Biochemistry, 2, 1449 (1963).
Kassell, B., Radicevic, M., Ansfield, M. J., and Laskowski, M., Biochem. Biophys. Res. Commun., 18, 255 (1965).
Gratecos, D., and Rovery, M., Biochim. Biophys. Acta, 140, 410 (1967).
Parkes, C. O., and Smillie, L. B., Canad. J. Biochem., 45, 1459 (1967).
Krehbiel, A., Kassell, B., and Laskowski, M., Biochim. Biophys. Acta, 92, 312 (1964).
Kubachi, V., Brown, K. D., and Laskowski, M., J. Biol. Chem., 180, 73 (1949).
Hartley, B. S., Nature, 201, 1284 (1964).
Parkes, C. O., and Smillie, L. B., Biochim. Biophys. Acta, 113, 629 (1966).
Hartley, B. S., and Kauffman, D. L., Biochem. J., 101, 229 (1966).
Fitch, W. M., and Margoliash, E., Science, 155, 279 (1967).
Guy, O., Rovery, M., and Desnuelle, P., Biochim. Biophys. Acta, 124, 402 (1966).
Perutz, M. F., Kendrew, J. C., and Watson, H. C., J. Mol. Biol., 13, 669 (1965).
Matthews, D. W., Sigler, P. B., Henderson, R., and Blow, D. M., Nature, 214, 652 (1967).
Sigler, P. B., and Blow, D. M., J. Mol. Biol. (in the press).
Mares-Guia, M., and Shaw, E., J. Biol. Chem., 240, 1579 (1965).
Bender, M. L., Killheffer, jun., J. V., and Kézdy, F. J., J. Amer. Chem. Soc., 86, 5331 (1964).
Smillie, L. B., and Hartley, B. S., Biochem. J., 101, 232 (1966).
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SMILLIE, L., FURKA, A., NAGABHUSHAN, N. et al. Structure of Chymotrypsinogen B compared with Chymotrypsinogen A and Trypsinogen. Nature 218, 343–346 (1968). https://doi.org/10.1038/218343a0
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DOI: https://doi.org/10.1038/218343a0
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