References
- Seemüller U., Meier M., Ohlsson K., Müller H. P., Fritz H. Hoppe Seyler's Z. Physiol. Chem. 1977; 358: 1105
- Seemüller U., Fritz H., Eulitz M. Methods Enzymol. 1981; 80: 804
- Seemüller U., Dodt J., Fink E., Fritz H. Proteinase Inhibitors, A. J. Barrett, G Salvesen. Elsevier, Amsterdam New York Oxford 1986; 336
- Chang J.-Y., Knecht R., Maschler R., Seemüller U. Biol. Chem. Hoppe-Seyler 1985; 366: 281
- Seemüller U., Eulitz M., Fritz H., Strobl A. Hoppe Seyler's Z. Physiol. Chem. 1980; 361: 1841
- McPhalen C. A., Schnebli H. P., James M. N.G. FEBS Letters 1985; 188: 55
- Bode W., Papamokos E., Musil D., Seemüller U., Fritz H. EMBO J. 1986; 5: 813
- Rink K., Liersch M., Sieber P., Meyer F. Nucleic Acids Res. 1984; 12: 6369
- Schnebli H. P., Seemüller U., Fritz H., Maschler R., Liersch M., Virca G. D., Bodmer J. L., Snider G. L., Lucey E. C., Stone P. G. Eur. J. Respir. Dis. 1985; 66(Suppl. 139)66
- Cohen A. B. Am. Rev. Respir. Dis. 1983; 127(Suppl. 2)S2
- Selected Topics in Clinical Enzymology, H. Fritz, M. Jochum, K.-H. Duswald, H. Dittmer, H. Kortmann, D. H. Goldberg, K. Werner. Walter de Gruyter and Co., Berlin New York 1984; Vol. 2: 305
- Janoff A. Annu. Rev. Med. 1985; 36: 207
- Markland F. S., Jr, Smith E. L. The Enzymes, P. D. Boyer. Academic Press, New York and London 1971; Vol. 3: 561
- Twumasi D. Y., Liener I. E. J. Biol. Chem. 1977; 252: 1917
- Antonini E., Ascenzi P., Bolognesi M., Gatti G., Guarneri M., Menegatti E. J. Mol. Biol. 1983; 165: 543
- Virca G. D., Metz G., Schnebli H. P. Eur. J. Biochem. 1984; 144: 1
- Finkenstadt W. R., Hamid M. A., Mattis J. A., Schrode J., Sealock R. W., Wang D., Laskowski M., Jr. Proteinase Inhibitors, H. Fritz, H. Tschesche, L. J. Greene, E. Truscheit. Springer-Verlag, Berlin, Heidelberg and New York 1974; 389
- Menegatti E., Guarneri M., Bolognesi M., Ascenzi P., Amiconi G. J. Mol. Biol. 1984; 176: 425
- Menegatti E., Guarneri M., Bolognesi M., Ascenzi P., Amiconi G. J. Mol. Biol. 1986; 191: 295
- Amiconi G., Ascenzi P., Bolognesi M., Menegatti E., Guarneri M. Macromolecular Biorecognition: Principles and Methods, I. M. Chaiken, E. Chiancone, A. Fontana, P. Neri. The Humana Press, Clifton 1987, in the press
- Tsukada M., Blow D. M. J. Mol. Biol. 1985; 184: 703
- Bode W., Wei A.-Z, Huber R., Meyer E., Travis J., Neumann S. EMBO J. 1986; 5: 2453
- , Amino acid residues have been identified by their 3-letter code and by their sequence number. The numbering of human leukocyte elastase22 and bovine α-chymotrypsin21.24 refers to that of bovine chymotrypsinogens A and B24. The numbering of subtilisin Carlsberg6,7 refers to that proposed by Edsall et al25
- Hartley B. S., Shotton D. M. The Enzymes, P. D. Boyer. Academic Press, New York and London 1971; Vol. 3: 323
- Edsall J. T., Flory P. J., Kendrew J. C., Liquori A. M., Nemethy G., Ramachandran G. N. J. Mol. Bid. 1966; 15: 399
- Ascenzi P., Menegatti E., Guarneri M., Bortolotti F., Antonini E. Biochemistry 1982; 21: 2483
- Bolognesi M., Ascenzi P., Amiconi G., Menegatti E., Guarneri M. Macromolecular Biorecognition: Principles and Methods, I. M. Chaiken, E. Chiancone, A. Fontana, P. Neri. The Humana Press, Clifton 1987, in the press
- , Although in the literature values of thermodynamic parameters for serine (pro)enzyme:inhibitor adduct formation are usually calculated from graphs of logK (M−1 or M) on 1/T,1–4,17–20 they should be only taken as apparent estimates.29 In fact, the application of the van't Hoffplot to a dimensioned equilibrium constant demands the use of relative concentrations, if a change in the mole number occurs in the reaction, and may imply oversimplified approximations.29 Therefore. according to Keleti.,29 values of thermodynamic parameters quoted in the present study. and obtained from plots of logKa, (M−1) on 1/T. are nominated as apparent quantities
- Keleti T. Biochem. J. 1983; 209: 277
- Baici A., Seemüller U. Biochem. J. 1984; 218: 829