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X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin

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Acid Proteases: Structure, Function, and Biology

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 95))

Abstract

Central to the study of mechanism and specificity of the acid proteinases is a knowledge of the three-dimensional structures of enzymes with different physiological roles. The availability of acid proteinases with either extracellular or intracellular roles in vertebrates as well as similar enzymes from plants, protozoa, and fungi allows a wide range of comparative studies. In our laboratory we have undertaken the x-ray analysis of fungal enzymes, those from Endothia parasitica and Mucor pusillus and some vertebrate enzymes including chymosin and chicken pepsin, and are beginning work with cathepsin D.

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References

  1. Hagemeyer, K., Fawwal, I., and Whitaker, J. R. (1968) J. Dairy Sci. 51, 1916–1930

    Article  Google Scholar 

  2. Sardinas, J. L. (1968) Appl. Microbiol. 16, 248–253

    CAS  PubMed  PubMed Central  Google Scholar 

  3. Williams, D. C., Whitaker, J. R., and Caldwell, P. V. (1972) Arch. Biochem. Biophys. 149, 52–61

    Article  CAS  Google Scholar 

  4. Moews, P. C., and Bunn, C. W. (1970) J. Mol. Biol. 54, 395–397

    Article  CAS  Google Scholar 

  5. Jenkins, J. A., Blundell, T. L., Tickle, I. J., and Ungaretti, L. (1975) J. Mol. Biol. 99, 583–590

    Article  CAS  Google Scholar 

  6. Bunn; C. W., Moews, P. C., and Baumber, M. E. (1971) Proc. R. Soc. London, B178, 245–258

    Google Scholar 

  7. Moews, P. C., and Bunn, C. W. (1972) J. Mol. Biol. 68, 389–390

    Article  CAS  Google Scholar 

  8. Green, M. L. (1975) Biochem. J. 151, 763–764

    Article  CAS  Google Scholar 

  9. Tickle, I. J. (1975) Acta Crystallogr. B31, 329–330

    Article  Google Scholar 

  10. North, A. C. T., Phillips, D. C., and Mathews, F. S. (1968) Acta Crystallogr. 24, 351–359

    Article  Google Scholar 

  11. Harding, M. D. (1962) Phil. Thesis, Oxford

    Google Scholar 

  12. Matthews, B. (1965) Acta Crystallogr. 20, 230–239

    Article  Google Scholar 

  13. Singh, A. K., and Ramaseshan, S. (1966) Acta Crystallogr. 21, 279–280

    Article  CAS  Google Scholar 

  14. Dodson, E. E., French, S., and Evans, P. (1975) in Anomalous Scattering (Ramaseshan, S. and Abraham, S. C., eds) pp. 423–426 Munkgaard International Publishers Ltd.

    Google Scholar 

  15. Blundell, T. L., and Johnson, L. N. (1976) Protein Crystallography, Academic Press, London

    Google Scholar 

  16. Dickerson, R. E., Kendrew, J. C., and Strandberg, B. E. (1961) Acta Crystallogr. 14, 1188–1195

    Article  CAS  Google Scholar 

  17. Blow, D. M., and Matthews, B. W. (1973) Acta Crystallogr. 29, 56–62

    Article  CAS  Google Scholar 

  18. Blow, D. M., and Crick, F. C. (1959) Acta Crystallogr. 12, 794–802

    Article  CAS  Google Scholar 

  19. North, A. C. T. (1965) Acta Crystallogr. 18, 212–216

    Article  CAS  Google Scholar 

  20. Subramanian, E., Swan, I. D. A., Liu, M., Davies, D. R., Jenkins, J. A., Tickle, I. J., and Blundell, T. L. PrOc. Natl. Acad. Sci. U.S.A., in press

    Google Scholar 

  21. Perimann, G. E., and Kerwar, G. A. (1973) Arch. Biochem. Biophys. 157, 145–147

    Article  Google Scholar 

  22. Grizzuti, K., and Perimann, G. E. (1969) J. Biol. Chem. 244, 1764–1776

    CAS  PubMed  Google Scholar 

  23. Chen, Y. H., Yang, J. T., and Chau, K. H. (1974) Biochemistry 13, 3350–3359

    Article  CAS  Google Scholar 

  24. Saxena, V. P., and Wetlaufer, D. B. (1971) Proc. Natl. Acad. Sci. U.S.A. 68, 969–972

    Article  CAS  Google Scholar 

  25. Greenfield, N., and Fasman, G. D. (1969) Biochemistry 8, 4108–4115

    Article  CAS  Google Scholar 

  26. Wang, T. T., Dorrington, K. J., and Hofmann, T. (1974) Biochem Biophys. Res. Commun. 57, 865–869

    Article  CAS  Google Scholar 

  27. Sepulveda, P., Marciniszyn, J., Liu, D., and Tang, J. (1975) J. Biol. Chem. 250, 5082–5088

    CAS  PubMed  Google Scholar 

  28. Foltmann, B., and Pedersen, V. B. Private Communication

    Google Scholar 

  29. Crowther, R. A. (1972) in Molecular Replacement Method (Rossmann, M. G. ed) Gordon ana Breacn, New York

    Google Scholar 

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Jenkins, J., Tickle, I., Sewell, T., Ungaretti, L., Wollmer, A., Blundell, T. (1977). X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin. In: Tang, J. (eds) Acid Proteases: Structure, Function, and Biology. Advances in Experimental Medicine and Biology, vol 95. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0719-9_4

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  • DOI: https://doi.org/10.1007/978-1-4757-0719-9_4

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  • Publisher Name: Springer, New York, NY

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  • Online ISBN: 978-1-4757-0719-9

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