Search Results - "Blech, Dianne M" :: K.UTB vyhledávací portál

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Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit

by Blech, Dianne M., Borders, C.L.
Published in Archives of biochemistry and biophysics (01.07.1983)

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L-amino acid ethyl ester hydrochlorides: Derivatives for qualitative organic analysis

by Borders, C. L, Blech, Dianne M, McElvany, Karen D
Published in Journal of chemical education (01.09.1984)

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Hydroperoxide anion, HO 2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit

by Blech, Dianne M., Borders, C.L.
Published in Archives of biochemistry and biophysics (15.07.1983)

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Reduced anion-binding affinity of Cu,Zn superoxide dismutases chemically modified at arginine

by Bermingham-McDonogh, Olivia, Mota de Freitas, Duarte, Kumamoto, Andrew, Saunders, Jan E., Blech, Dianne M., Borders, C.L., Valentine, Joan S.
Published in Biochemical and biophysical research communications (29.10.1982)

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Journal Article

Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit

L-amino acid ethyl ester hydrochlorides: Derivatives for qualitative organic analysis

Hydroperoxide anion, HO 2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit

Reduced anion-binding affinity of Cu,Zn superoxide dismutases chemically modified at arginine

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