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Molecular modeling and electrostatic potential calculations on chemically modified Cu,Zn superoxide dismutases from Bos taurus and shark Prionace glauca: role of Lys134 in electrostatically steering the substrate to the active site. Archives of Biochemistry and Biophysics, 312(1), 22–30
DOI: 10.1006/abbi.1994.1275
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A comparative study on the anion binding properties of Bos taurus and Prionace glauca Cu,Zn superoxide dismutases native and chemically modified at lysines. Comparative Biochemistry and Physiology – Part C, Pharmacology, Toxicology and Endocrinology, 109(2), 141–145
DOI: 10.1016/0742-8413(94)00052-C
The effect of phenylglyoxal on Cu, Zn superoxide dismutase from the shark Prionace glauca. Italian Journal of Biochemistry, 39(3), 207–208
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Substitution of arginine for lysine 134 alters electrostatic parameters of the active site in shark Cu,Zn superoxide dismutase. FEBS Letters, 250(1), 49–52
DOI: 10.1016/0014-5793(89)80682-9