Abstract
AbstractA preparation of the protein subunits from calf neurofilaments has been obtained. Axon segments from an homogenate of calf brain white matter have been concentrated by a subcellular fractionation procedure. After further steps to achieve a complete elimination of unbound lipid, the neurofilament protein was dissolved in 4M guanidine hydrochloride solutions. The neurofilalment subunit was the major constituent of the guanidine hydrochloride extracts; other proteins of higher molecular weight were eliminated by agarose gel filtration in urea solutions. Dialysis to solutions of low ionic strength allowed the reformation of fibril aggregates, some of which, under electron microscopy, resembled the original neurofilaments in morphology.The physical characteristics of the neurofilament subunit protein are reported and a preliminary amino acid analysis is given. The neurofilament protein is clearly distinguishable from actin and tubulin on physical and chemical grounds.
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