Myelin basic protein is a zinc-binding protein in brain: Possible role in myelin compaction
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AbstractThe zinc-binding proteins (ZnBPs) in porcine brain were characterized by the radioactive zinc-blot technique. Three ZnBPs of molecular weights about 53 kDa, 42 kDa, and 21 kDa were identified. The 53 kDa and 42 kDa ZnBPs were found in all subcellular fractions while the 21 kDa ZnBP was mainly associated with particulate fractions, This 21 kDa ZnBP was identified by internal protein sequence data as the myelin basic protein. Further characterization of its electrophoretic properties and cyanogen bromide cleavage pattern with the authentic protein confirmed its identity. The zinc binding properties of myelin basic protein are metal specific, concentration dependent and pH dependent. The zinc binding property is conferred by the histidine residues since modification of these residues by diethyl-pyrocarbonate would abolish this activity. Furthermore, zinc ion was found to potentiate myelin basic protein-induced phospholipid vesicle aggregation. It is likely that zinc plays an important role in myelin compaction by interacting with myelin basic protein.
All Author(s) ListTsang D, Tsang YS, Ho WKK, Wong RNS
Journal nameNeurochemical Research
Year1997
Month7
Day1
Volume Number22
Issue Number7
PublisherSPRINGER/PLENUM PUBLISHERS
Pages811 - 819
ISSN0364-3190
LanguagesEnglish-United Kingdom
Keywordsmyelin; myelin basic protein; porcine brain; zinc-binding protein
Web of Science Subject CategoriesBiochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Neurosciences; NEUROSCIENCES; Neurosciences & Neurology

Last updated on 2020-23-10 at 02:04