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Structure-Function Database for Active Site Binding to the Aspartic Proteinases

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Structure and Function of the Aspartic Proteinases

Abstract

Aspartic Proteinases are produced in the human body by a variety of cells. Some of these proteins, for example, pepsin, gastricsin and renin are secreted and exert their effects in the extracellular spaces. Cathepsin D and cathepsin E, on the other hand, are intracellular enzymes.

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References

  • Abad-Zapatero, C., Rydel, T. J., Neidhart, D. J., Luly, J. and Erickson, J. W., Inhibitor binding induces structural changes in porcine pepsin, in: “Structure and Function of the Aspartic Proteinases: Genetics, Structures and Mechanisms,” Ben M. Dunn, ed., Plenum Press, New York.

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  • Afting, E. G. and Becker, M. L., 1981, Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield, Biochem. J. 197: 519–522.

    PubMed  CAS  Google Scholar 

  • Dunn, B. M, Jiminez, M, Parten, B. F., Valier, M. J., Rolph, C. E. and Kay, J., 1986, A systemic series of synthetic chromophoric substrates for aspartic proteinases, Biochem. J. 237: 899–906.

    PubMed  CAS  Google Scholar 

  • Pohl, J. and Dunn, B. M., 1988, Secondary enzyme-substrate interactions: Kinetic evidence for ionic interactions between substrate side chains and the pepsin active site, Biochemistry 27: 4827–4834.

    Article  PubMed  CAS  Google Scholar 

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© 1991 Plenum Press, New York

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Rao, C. et al. (1991). Structure-Function Database for Active Site Binding to the Aspartic Proteinases. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_19

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  • DOI: https://doi.org/10.1007/978-1-4684-6012-4_19

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-6014-8

  • Online ISBN: 978-1-4684-6012-4

  • eBook Packages: Springer Book Archive

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