- 1) Endo, S., Study on protease by thermophilic bacteria. J. Ferment. Technol. (in Japanese), 40, 346–353 (1962).
- 2) Inouye, K., Thermolysin. In “Handbook of Food Enzymes,” eds. Whitaker, J. R., Voragan, A. G. J., and Wong, D. W. S., Marcel Dekker, New York, pp. 1019–1028 (2003).
- 3) Van den Burg, B., and Eijsink, V., Thermolysin. In “Handbook of Proteolytic Enzymes” 2nd ed. Vol. 1, eds. Barrett, J. A., Rawlings, N. D., and Woessner, J. F., Elsevier, Amsterdam, pp. 374–387 (2004).
- 4) Pangburn, M. K., Burstein, Y., Morgan, P. H., Walsh, K. A., and Neurath, H., Affinity chromatography of thermolysin and of neutral proteases from B. subtilis. Biochem. Biophys. Res. Commun., 54, 371–379 (1973).
- 5) Walsh, K. A., Burstein, Y., and Pangburn, M. K., Thermolysin and other neutral metalloendopeptidases. In “Methods in Enzymology” Vol. 34, eds. Jakoby, W. B., and Wilchek, M., Academic Press, New York, pp. 435–440 (1974).
- 6) Van den Burg, B., Eijsink, V. G., Stulp, B. K., and Venema, G., One-step affinity purification of Bacillus neutral proteases using Bacitracin-silica. J. Biochem. Biophys. Methods, 18, 209–220 (1989).
- 7) Morihara, K., and Tsuzuki, H., Thermolysin: kinetic study with oligopeptides. Eur. J. Biochem., 15, 374–380 (1970).
- 8) Inouye, K., Lee, S.-B., and Tonomura, B., Effect of amino acid residues at the cleavage site of substrates on the remarkable activation of thermolysin by salts. Biochem. J., 315, 133–138 (1996).
- 9) O’Donobue, M. J., Roques, B. P., and Beaumont, A., Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin. Biochem. J., 300, 599–603 (1994).
- 10) Inouye, K., Minoda, M., Takita, T., Sakurama, H., Hashida, Y., Kusano, M., and Yasukawa, K., Extracellular production of recombinant thermolysin expressed in Escherichia coli, and its purification and enzymatic characterization. Protein Expr. Purif., 46, 248–255 (2006).
- 11) Yasukawa, K., Kusano, M., Nakamura, K., and Inouye, K., Characterization of Gly-D-Phe, Gly-L-Leu, and D-Phe as affinity ligands to thermolysin. Protein Expr. Purif., 46, 332–336 (2006).
- 12) Nakamura, K., Suzuki, T., Hasegawa, M., Kato, Y., Sasaki, H., and Inouye, K., Characterization of p-aminobenzamidine-based sorbent and its use for high-performance affinity chromatography of trypsin-like proteases. J. Chromotogr. A, 1009, 133–139 (2003).
- 13) Inouye, K., Effects of salts on thermolysin: activation of hydrolysis and synthesis of N-carbobenzoxy-L-asparatyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. J. Biochem., 112, 335–340 (1992).
- 14) Langmuir, I., The adsorption of gases on plane surfaces of glass, mica and platinum. J. Am. Chem. Soc., 40, 1361–1403 (1948).
- 15) Naumann, M., Reuter, R., Metz, P., and Kopperschlager, G., Affinity chromatography of bovine heart lactate dehydrogenase using dye ligands linked directly or spacer-mediated to bead cellulose. J. Chromatogr., 466, 319–329 (1989).
- 16) Vaidya, A. A., Lele, B. S., Kulkarni, M. G., and Mashelkar, R. A., Enhancing ligand-protein binding in affinity thermoprecipitation: elucidation of spacer effects. Biotechnol. Bioeng., 64, 418–425 (1999).
- 17) Morimoto, K., and Inouye, K., Single-step purification of F(ab′)2 fragments of mouse monoclonal antibodies (immunoglobulins G1) by hydrophobic interaction high performance liquid chromatography using TSKgel Phenyl-5PW. J. Biochem. Biophys. Methods, 24, 107–117 (1992).
- 18) Nakamura, K., Suzuki, T., Kamichika, T., Hasegawa, M., Kato, Y., Sasaki, H., and Inouye, K., Evaluation and applications of a new dye affinity adsorbent. J. Chromatogr. A, 972, 21–25 (2002).
Bioscience, Biotechnology, and Biochemistry
Volume 71, 2007 - Issue 8