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Title: 200 Kd neurofilament protein binds Al, Cu and Zn.

Authors: Pierson, K B; Evenson, M A

Published In Biochem Biophys Res Commun, (1988 Apr 29)

Abstract: 200 Kd human and bovine neurofilament proteins were isolated from spinal cord and purified to homogeneity. The purified proteins were shown to be metal-binding proteins which bind at least one mole of Al, one mole of Cu and four moles of Zn. Neither dephosphorylation of the protein nor equilibrium dialysis against 25 mM EDTA, pH 7.0, removed these metals. This is the first report of a human protein which stoichiometrically binds Al.

PubMed ID: 3130052 Exiting the NIEHS site

MeSH Terms: Aluminum/metabolism; Animals; Carrier Proteins/isolation & purification; Carrier Proteins/metabolism*; Cattle; Copper/metabolism; Humans; Intermediate Filament Proteins/isolation & purification; Intermediate Filament Proteins/metabolism*; Metals/metabolism*; Molecular Weight; Neurofilament Proteins; Spinal Cord; Zinc/metabolism

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