Involvement of both a Zn2+ site and an anionic binding site in the selective inhibition of a Zn2+-glycerophosphocholine cholinephosphodiesterase by thiols and tellurites
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cellular and Molecular Neuroscience,General Medicine,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/BF00970539.pdf
Reference21 articles.
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2. Sok, D.-E., and Kim, M. R. 1992. A spectrophotometric assay of Zn2+-glycerophosphorylcholine phosphocholine phosphodiesterase using ?-nitrophenylphosphorylcholine. Anal. Biochem. 203: 201?205.
3. Sok, D.-E., and Kim, M. R. 1992. Characterization of a Zn2+-requiring glycerophosphocholine cholinephosphodiesterase possessing ?-nitrophenylphosphocholine phosphodiesterase activity. Biochem. J. 286:435?440.
4. Janzen, L., Tourtellotte, W. W., and Kanfer, J. N. 1990. Glycerylphosphocholine phosphocholine phosphodiesterase activity is reduced in multiple sclerosis plaques. Exp. Neurol. 109:243?246.
5. Spanner, S., and Ansell, G. B. 1987. The hydrolysis of glycerophosphorylcholine by rat brain microsomes: activation and inhibition. Neurochem. Res. 12:203?206.
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