Methods in Molecular Biology • 16 Enzymes of Molecular Biology

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  1. Drapeau, G. R. (1977) Cleavage at glutamic acid with staphlococcal protease.
    Methods Enzymol. 47, 189-191.

  2. Jekei, P. A., Weijer, W. J., and Beintema, J. J. (1983) Use of endoproteinase
    Lys-C from Lysobacter enzymogenes in protein sequence analysis. Anal.
    Biochem. 134, 347-354.

  3. Fruton, J. S. (1971) Pepsin. Enzymes 4, 120-164.

  4. Tang, J. (1970) Gastricsin and pepsin. Methods Enzymol. 19, 406-421.

  5. Rajagopalan, T. G., Moore, S., and Stein, W. H. (1966) Pepsin from pepsino-
    gen. Purification and properties. J. Biol. Chem. 241, 4940-4950.

  6. Perimann, G. E. (1959) Effect of solvents and of temperature on the optical
    rotary properties of pepsin. Proc. Natl. Acad. Sci. USA 45, 915-922.

  7. Matsubara, H. (1970) Purification and assay of thermolysin. Methods Enzymol.
    19, 642-651.

  8. Heinrikson, R. L. (1977) Applications of thermolysin in protein structural analy-
    sis. Methods Enzymol. 47, 75-189.

  9. Matsubara, H., Sasaki, R., Singer, A., and Jukes, T. H. (1966) Specific nature
    of hydrolysis of insulin and tobacco mosaic virus protein by thermolysin. Arch.
    Biochem. Biophys. 115, 324-331.

  10. Titani, K., Hermodson, M. A., Ericson, L. H., Walsh, K. A., and Neurath, H.
    (1972) Amino acid sequence of thermolysin. Nature 238, 35-37.

  11. Latt, S. A., Holmquist, B., and Vallee, B. L. (1969) Thermolysin: A zinc
    metalloenzyme. Biochem. Biophys. Res. Commun. 37, 333-339.

  12. Walsh, K. A. (1970) Trypsinogens and trypsins of various species. Methods
    Enzymol. 19, 41-63.

  13. Mares-Guia, M. and Shaw, E. (1965) Studies on the active center of trypsin. J.
    Biol. Chem. 240, 1579-1585.

  14. Harris, J. I. (1956) Effect of urea on trypsin and a-chymotrypsin. Nature 177,
    471-473.

  15. Anson, M. L. (1938) Estimation of pepsin, trypsin, papain and cathepsin with
    haemoglobin. J. Gen. Physiol. 22, 79-89.

  16. Schwert, G. W. and Eisenberg, M. A. (1949) Kinetics of the amidase and esterase
    activities of trypsin. J. Biol. Chem. 179, 665-672.

  17. Nord, F. F. and Bier, M. (I 953) Mechanism of enzyme action. LV. Interaction
    between calcium and trypsin. Biochem.Biophys. Acta 12, 56-60.

  18. Birk, Y. (1961) Purification and some properties of a highly active inhibitor of
    trypsin and ~-chymotrypsin from soybeans. Biochim. Biophys. Acta 54, 378-381.

  19. Shaw, E. and Springhorn, S. (1967) Identification of the histidine residue at
    the active center of trypsin labeled by TLCK. Biochem. Biophys. Res. Commun.
    27, 391-397.

  20. Carrey, E. A. and Epand, R. M. (1983) Conformational and biological proper-
    ties of glucagon fragments containing residues 1-17 and 19-29. J. Peptide Pro-
    tein Res. 22, 362-370.

  21. Grunnet, I. and Knudsen, J. (1983) Medium-chain fatty acid synthesis by goat
    mammary-gland fatty acid synthetase. The effect of limited proteolysis. Biochem.
    J. 209, 215-222.

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