References
- Proteases and Biological Control, E. Reich, D.B. Rifkin, E. Shaw. Cold Spring Harbor Laboratory, Cold Spring Harbor and New York 1975
- Proteolysis and Physiological Regulation, D. W. Ribbons, K. Brew. Academic Press, New York. San Francisco and London 1976
- Proteases: Potential Role in Health and Diseases, H. Hörn, A. Heidland. Plenum Press, New York and London 1982
- Proteases in Biological Control and Biotechnology, D. D. Cunningham, G.L. Long. Alan R. Liss. Inc., New York 1986
- Enzyme Inhihitors as Drugs, A. J. Barrett, M. Sandier. McMillan, London 1980
- Schebli H.-P., Braun N.J. Proteinase Inhibitors, A. J. Barrett, G. Salvesen. Elsevier, Amsterdam. New York and Oxford 1986; 614
- Tamura Y., Hirado H., Okamura K., Minato Y., Fujii S. Biochim. Biophys. Acta 1977; 484: 417
- Ohno H., Kosaki J., Kambayashi J., Imaoka S., Hirata F. Thromb. Res. 1980; 19: 579
- Mennegatti E., Scalia S., Bortolotti F., Ascenzi P., De A., Marco M. Guarneri. Pharm. Acta Helv. 1985; 60: 170
- Menegatti E., Bolognesi M., Scalia S., Bortolotti F., Guarneri M., Ascenzi P. J. Pharm. Sci. 1986; 75: 1171
- The Enzymes 3rd edn, B.S. Hartley, D.M. Shotton, P.D. Boyer. Academic Press, New York and London 1971; Vol. 3: 323
- Titani K., Fujikawa K., Enfield D.L., Ericsson L.H., Walsh K.A., Neurath H. Proc. Natl. Acad. Sci. U.S.A. 1975; 72: 3082
- Castellino F. J., Powell J. R. Meth. Enzymol. 1981; 80: 365
- Bode W., Chen Z, Bartels K., Kutzback C., Schmidt-Kastner G., Bartunik H. J. Mol. Biol. 1983; 164: 237
- Kasai S., Arimura H., Nishida M., Sujama T. J. Biol. Chem. 1985; 260: 12382
- Fukushima D., Kitamura N., Nakanishi S. Biochemistry 1985; 24: 8037
- Bode W., Schwager P. J. Mol. Biol. 1975; 98: 693
- Huber R., Bode W. Acc. Chem. Res. 1978; 11: 114
- Furie B., Bing D.H., Feldmann R.J., Robison D.J., Burnier J. P., Furie B.C. J. Biol. Chem. 1982; 257: 3875
- Bode W., Walter J., Huber R., Wenzel H. R., Tschesche H. Eur. J. Biochem. 1984; 144: 185
- Chen Z., Bode W. J. Biol. Chem. 1983; 164: 283
- Bing D.H., Feldmann R. J., Fenton J.W., II. Ann. N.Y. Acad. Sci. 1986; 485: 104
- Bolognesi M., Ascenzi P., Amiconi G., Menegatti E., Guarneri M. Macromolecular Biorecognition: Principles and Methods, I. M. Chaiken, E. Chiancone Neri, P A. Fontana. The Humana Press, Clifton 1987; p81
- Ascenzi P., Torroni A., Menegatti E., Guarneri M., Amiconi G. Biochim. Biophys. Acta 1985; 832: 215
- Lundblad R.L., Kingdon H. S., Mann K.G. Meth. Enzyniol. 1976; 45: 156
- Nolan C., Hall L. S., Barlow G.H. Methods Enzymol. 1976; 45: 205
- Markland F.S., Jr. Meth. Enzymol. 1976; 45: 223
- Luthy J.A., Praissman M., Finkenstadt W. R., Laskowski M., Jr. J. Biol. Chem. 1973; 248: 1760
- Fiedler F., Fink E., Tschesce H., Fritz H. Meth. Enzymol. 1981; 80: 493
- Geigner R., Fritz H. Meth Enzymol. 1981; 80: 466
- Barlow G.H. Meth. Enzymol. 1976; 45: 239
- Glass J. D., Pe1zig M. Int. J. Pept. Protein Res. 1978; 12: 75
- Jesty J., Nemerson Y. Meth. Enzymol. 1976; 45: 95
- Ascenzi P., Sleiter G., Antonini E. Gazz. Chem. Ital. 1982; 112: 307
- Ascenzi P., Bertollini A., Bolognesi M., Guarneri M., Menegatti E., Amiconi G. Biochim. Biophys. cta. 1986; 871: 225
- Ascenzi P., Ascenzi M. P., Amiconi G. Biochem. Educution 1987; 15: 134
- Sagnella G.A. Treticls Biochem. Sci. 1985; 10: 100
- Jones T.A. J. Appl. Crystallogr. 1978; 11: 268
- Bernstein F.C., Koetzle T.F., Williams G.J.B., Majer E. F., Jr., Brice M.D., Rogers J.R., Kennard O., Shimanouchi T., Tasumi M. J. Mol. Biol. 1977; 112: 535
- Pirkle H., Markland F. S., Jr., Theodor I., Baumgartner R., Bajwa S. S., Kirakossian H. Biochem. Biophys Res. Commun. 1981; 99, 715
- McGillavry C. H., Rieck G.D. International Tables for X-ray Crystallography, K. Lansdale. Kynoch Press, Birmingham 1962; Vol. 3
- Wyman J. Adv. Protein Chem 1964; 19: 223
- Laskowski M., Jr., Kato I. Annu. Rev. Biochem. 1980; 49: 598
- Ascenzi P., Menegatti E., Guarneri M., Bortollotti F., Antonini E. Biochemistry 1982; 21: 2483
- Ascenzi P., Bertollini A, Bolognesi M., Guarneri M., Menegatti E., Antonini E. Proteinase Action, P. Elödi. Akadémiai Kiadó, Budapest 1984; p339
- Amiconi G., Ascenzi P., Bolognesi M., Menegatti E., Guarneri M. Macromolecular Biorecognition: Principles and Methods, I. M. Chaiken, E. Chiancone Neri, P. A. Fontana. The Humana Press, Clifton 1987; p117
- Menegatti E., Guarneri M., Bolognesi M., Ascenzi P., Amiconi G. Macromolecular Biorecognition: Principles and Methods, I.M. Chaiken, E. Chiancone, P. Neri, A. Fontana. The Humana Press, Clifton 1987; p101
- Amino acid residues have been identified by their three-letter code and by their sequence number. The numbering of human Lys77-plasmin refers to that of the complete form (Glu1) of human plasminogen.13 The numbering of bovine factor xa refers to that of its heavy chain.12 The numbering of bovine α-thrombin, bovineβ-trypsin, porcine pancreatic β-kallikrein-B and human urinary kallikrein refers to that of bovine chymotrypsinogens A and B.11. The numbering of the Mr 54,000 species of human urokinase refers to that of the single-chain pro-urokinase.15
- The pK values of the -guanidino and -amino group of -GCA-CEP and -ACA-CEP. respectively, are higher than 10; therefore, over the whole pH range explored (2.0 to 8.5), the inhibitors examined are always in the cationic form. 10
- Powers J. C., Harper J.W. Proteinase Inhibitors, A. J. Barrett, G. Salvesen. Elsevier, Amsterdam, New York and Oxford 1986; 55