Abstract
Purified mast cell carboxypeptidase cleaved the C-terminal leucines from Leu 5-enkephalin (Leu-ENK), neurotensin (NT), and kinetensin (KT), with K m values of 36, 16, and 15 μM, and k cat values of 44, 51, and 53 s −1, respectively. To better predict potential in vivo hydrolysis products generated by mast cell proteases, these peptides were incubated with released skin mast cell supernatants. Leu 5-enkephalin was hydrolyzed only by carboxypeptidase. Kinetensin was cleaved by tryptase, chymase, and carboxypeptidase to yield KT(1–3), KT(1–7), KT(1–8), KT(4–7), and KT(4–8), the last two peptides by the concerted action of two of the proteases. NT(1–11) and NT(1–12) were generated from neurotensin by chymase and carboxypeptidase, respectively.
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