Isolation of a stable tetramer of the low molecular weight component of neurofilaments (NF-L)

Journal of Biochemistry
S Tokutake, K Tanaka

Abstract

When crude neurofilaments were dissolved in a solution containing 8 M urea and 1% beta-mercaptoethanol (beta-ME), the component proteins of the neurofilaments and other contaminating filaments were solubilized into monomeric forms. However, when reassembled filaments were solubilized again by the addition of urea to 8 M without beta-ME, several bands which seemed to be oligomeric forms of filament proteins were observed on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Among them, a band which appeared between microtubule-associated protein-1 (MAP-1) and fodrin was most remarkable. This band was also observed when a triplet mixture of the neurofilaments (NF-H, NF-M, NF-L) was reassembled. The molecular weight of this band was estimated to be 280 kDa. In addition, much of this component was easily isolated on DE-52 column chromatography of the reassembled crude neurofilament proteins with buffers containing 6 M urea, while the low molecular weight component of the neurofilaments (NF-L, 70 kDa) was hardly detected. Furthermore, the isolated 280 kDa component was reduced to NF-L on the addition of beta-ME to 1%. In contrast, the 280 kDa component was produced on dialysis of isolated NF-L against the assembly...Continue Reading

Citations

Jan 1, 1990·The International Journal of Biochemistry·S Tokutake

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