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Enzymatically active zinc, copper and mercury derivatives of the one-iron form of pig allantoic fluid acid phosphatase

Journal Article


Abstract


  • Derivatives of the violet, iron-containing acid phosphatase of pig allantoic fluid have been prepared in which one of the two iron atoms present in the native enzyme has been replaced by zinc, copper or mercury. The derivatives so formed are enzymatically active: the Zn-Fe, Cu-Fe and Hg-Fe enzymes have specific activities of about 80%, 25% and 17% respectively, of the maximum specific activity of the Fe-Fe enzyme in the standard assay at pH 4.9 with p-nitrophenyl phosphate as substrate. In contrast to the Fe-Fe enzyme, the mixed metal derivatives are not rapidly inactivated by H2O2. Visible absorption spectra of the derivatives confirm that all of the visible absorption of the Fe-Fe enzyme is due to one of the iron atoms. Attempts to prepare an active Cu-Cu enzyme were unsuccessful. © 1984.

Publication Date


  • 1984

Citation


  • Beck, J. L., Keough, D. T., Jersey, J. D., & Zerner, B. (1984). Enzymatically active zinc, copper and mercury derivatives of the one-iron form of pig allantoic fluid acid phosphatase. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 791(3), 357-363. doi:10.1016/0167-4838(84)90347-9

Scopus Eid


  • 2-s2.0-0021744038

Start Page


  • 357

End Page


  • 363

Volume


  • 791

Issue


  • 3

Abstract


  • Derivatives of the violet, iron-containing acid phosphatase of pig allantoic fluid have been prepared in which one of the two iron atoms present in the native enzyme has been replaced by zinc, copper or mercury. The derivatives so formed are enzymatically active: the Zn-Fe, Cu-Fe and Hg-Fe enzymes have specific activities of about 80%, 25% and 17% respectively, of the maximum specific activity of the Fe-Fe enzyme in the standard assay at pH 4.9 with p-nitrophenyl phosphate as substrate. In contrast to the Fe-Fe enzyme, the mixed metal derivatives are not rapidly inactivated by H2O2. Visible absorption spectra of the derivatives confirm that all of the visible absorption of the Fe-Fe enzyme is due to one of the iron atoms. Attempts to prepare an active Cu-Cu enzyme were unsuccessful. © 1984.

Publication Date


  • 1984

Citation


  • Beck, J. L., Keough, D. T., Jersey, J. D., & Zerner, B. (1984). Enzymatically active zinc, copper and mercury derivatives of the one-iron form of pig allantoic fluid acid phosphatase. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 791(3), 357-363. doi:10.1016/0167-4838(84)90347-9

Scopus Eid


  • 2-s2.0-0021744038

Start Page


  • 357

End Page


  • 363

Volume


  • 791

Issue


  • 3