Add time:08/14/2019         Source:sciencedirect.com

The stability of neurotensin (NT) and a potent, long lasting analogue, [d-Trp11]-NT, to rat brain peptidases was compared by incubating the peptides with subcellular fractions (synaptosomes, synaptic membranes) and a purified endopeptidase from rat brain. Degradation of the peptides with time was followed by high performance liquid chromatography (HPLC). The rates of degradation (pmol/min/mg prot.) in synaptosomes were 890 (NT) and 59 [d-Trp11]-NT), and in synaptic membranes were 1180 (NT) and 12 ([d-Trp11]-NT). The main products of the degradation of [d-Trp11]-NT by synaptic peptidases (isolated by HPLC and characterized by amino acid analysis) were the 1–3, 1–4 and 6–13 fragments implying cleavage of [d-Trp11]-NT at the Tyr3-Glu4, Glu4-Asn5 and Asn5-Lys6 bonds. The rates of degradation of NT and [d-Trp11]-NT by the purified endopeptidase from rat brain were 27.2 and 0.76 pmol/min/μl of enzyme solution respectively. This endopeptidase, which hydrolyses NT at Arg8-Arg9, may be responsible along with other endopeptidases for NT degradation at nerve terminals.

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