Abstract
The renal and intestinal brush border membranes are an abundant source of peptidase and proteinase activities, most of which are zinc metalloenzymes (see e.g. Kenny et al., 1987). These membranes have proved valuable as starting material for purification of these enzymes as well as for investigating their likely physiological functions. Such studies have been much aided by a range of selective and potent peptidase inhibitors, mainly of microbial origin. In the human renal brush border there is only one identified endopeptidase, an activity now referred to as endopeptidase-24.11 (E-24.11) or neprilysin (EC 3.4.24.11). E-24.11 was first purified to homogeneity and characterised some twenty years ago (Kerr & Kenny, 1974) as an insulin B chain degrading activity, although the physiological role of the enzyme was unknown. In the intervening time, several key substrates for the enzyme have been described, the localization of the enzyme explored in considerable detail and other members of the mammalian E-24.11 gene family have recently been reported.
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© 1996 Plenum Press, New York
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Turner, A.J., Murphy, L.J., Medeiros, M.S., Barnes, K. (1996). Endopeptidase-24.11 (Neprilysin) and Relatives. In: Suzuki, K., Bond, J.S. (eds) Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology, vol 389. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0335-0_17
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DOI: https://doi.org/10.1007/978-1-4613-0335-0_17
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