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

Beck J.L., Keough D.T., Jersey J.D. and 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


Author Beck J.L.
Keough D.T.
Jersey J.D.
Zerner B.
Title Enzymatically active zinc, copper and mercury derivatives of the one-iron form of pig allantoic fluid acid phosphatase
Journal name Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
ISSN 0167-4838
Publication date 1984-12-21
Sub-type Article (original research)
DOI 10.1016/0167-4838(84)90347-9
Volume 791
Issue 3
Start page 357
End page 363
Total pages 7
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
1315 Structural Biology
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of pig allantoic fluid have been prepared in which one of the two iron atoms present in the native enzyme has been replaced by zinc, copper or mercury.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.
Keyword (Pig allantoic fluid)
Acid phosphatase
Iron protein
Metal-ion substitution
Uteroferrin
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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