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Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase

✍ Scribed by Hercilia M. Molina; Adriana K. Carmona; Maria Kouyoumdjian; Durval R. Borges

Book ID
117172404
Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
341 KB
Volume
67
Category
Article
ISSN
0024-3205

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Regulators of the neuropeptide-degrading
Regulators of the neuropeptide-degrading enzyme, EC 3.4.24.15 (thimet oligopeptidase), in cerebrospinal fluid
✍ Corie N. Shrimpton; Adele J. Wolfson; A. Ian Smith; Rebecca A. Lew πŸ“‚ Article πŸ“… 2003 πŸ› John Wiley and Sons 🌐 English βš– 73 KB

## 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

Selective Neurotensin-Derived Internally
Selective Neurotensin-Derived Internally Quenched Fluorogenic Substrates for Neurolysin (EC 3.4.24.16): Comparison with Thimet Oligopeptidase (EC 3.4.24.15) and Neprilysin (EC 3.4.24.11)
✍ Vitor Oliveira; Marcelo Campos; Jefferson P. Hemerly; Emer S. Ferro; Antonio C.M πŸ“‚ Article πŸ“… 2001 πŸ› Elsevier Science 🌐 English βš– 86 KB

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