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- W2027791930 abstract "Axonal transport of Boc-Arg-Val-Arg-Arg-MCA hydrolyzing enzyme activity was studied in rat sciatic nerves from 12 to 120 h after double ligations. The anterograde axonal transport increased and peaked 72 h after ligation. The optimum pH for Boc-Arg-Val-Arg-Arg-MCA hydrolyzing enzyme activity was 6.5 to 6.9 and did not require Ca(2+) for the activity. Two molecular forms with enzyme activity were identified by size-exclusion chromatography and the molecular masses of the two enzymes were estimated to be 98 and 52 kDa. Two enzyme activities were strongly inhibited by Hg(2+), Cu(2+) and trypsin inhibitors such as TLCK, antipain and leupeptin. It cleaved the substrate, Boc-Arg-Val-Arg-Arg-MCA, between the dibasic sequence Arg-Arg, and needed a support of aminopeptidase B-like enzyme activity for the liberation of 7-amino-4-methylcoumarin. These results suggest that the enzyme is transported in rat sciatic nerves and involved in the post-translational processing of precursor proteins under the anterograde axonal transport. But there is absolutely no evidence for a role in precursor processing and such a putative role is purely speculative." @default.
- W2027791930 created "2016-06-24" @default.
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- W2027791930 date "2000-02-01" @default.
- W2027791930 modified "2023-10-18" @default.
- W2027791930 title "Anterograde axonal transport of Boc-Arg-Val-Arg-Arg-MCA hydrolyzing enzyme in rat sciatic nerves: cleavage occurs between basic residues" @default.
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- W2027791930 doi "https://doi.org/10.1016/s0167-4838(99)00239-3" @default.
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