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- W1996906246 abstract "Functions of the tail region of neurofilament L have, to date, not been clearly elucidated. Bovine neurofilament L was cleaved into tail-less neurofilament L (50 kDa) and a tail fragment (19 kDa), by thrombin. Tail-less neurofilament L was deficit of the highly acidic domain of the tail region (approximately 77% of the entire region). Assembly of tail-less neurofilament L. was observed to be accelerated by both fluorometric and centrifugal measurements, compared with intact neurofilament L. The critical concentration of tail-less neurofilament L, which constitutes the constant unassembled pool, was approximately 0.25-times lower than that of neurofilament L. Under physiological conditions, tail-less neurofilament L formed a ribbon-like structure, whereas tail-less neurofilament L could form 10-nm filaments in an extremely low ionic-strength buffer in the presence of 1 mM MgCl2. An affinity-purified antibody directed against the tail fragment also accelerated neurofilament L assembly. The tail fragment neither coassembled with neurofilament L nor affect neurofilament L assembly. The acidic domain of the tail region may regulate neurofilament assembly and may be involved in 10-nm filament formation under physiological conditions." @default.
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- W1996906246 date "1993-03-01" @default.
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- W1996906246 title "Acceleration of bovine neurofilament L assembly by deprivation of acidic tail domain" @default.
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- W1996906246 doi "https://doi.org/10.1111/j.1432-1033.1993.tb17694.x" @default.
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