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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
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.
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.
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.
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.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Plenum Press, New York
About this chapter
Cite this chapter
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
Download citation
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