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Differential subcellular distribution of neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) in the rat brain

✍ Scribed by Eduardo E Massarelli; Cláudio A Casatti; Akira Kato; Antonio C.M Camargo; Jarbas A Bauer; Marc J Glucksman; James L Roberts; Shigehisa Hirose; Emer S Ferro

Book ID
114005452
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
382 KB
Volume
851
Category
Article
ISSN
0006-8993

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Internally quenched fluorescent peptides derived from neurotensin (pELYENKPRRPYIL) sequence were synthesized and assayed as substrates for neurolysin (EC 3.4.24.16), thimet oligopeptidase (EC 3.4.24.15 or TOP), and neprilysin (EC 3.4.24.11 or NEP). Abz-LYENKPRRPYILQ-EDDnp (where EDDnp is N-(2,4-dini

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## Abstract Endopeptidase EC 3.4.24.15 (EP 24.15; thimet oligopeptidase) is a soluble metalloendopeptidase implicated in the metabolism of a number of neuropeptides, including neurotensin, gonadotropin‐releasing hormone, and opioid peptides. We have shown previously that thiol reducing agents, such