Iron-containing acid phosphatases: Characterization of the metal-ion binding site of the enzyme from pig allantoic fluid

Keough D.T., Dionysius D.A., de Jersey J. and Zerner B. (1980) Iron-containing acid phosphatases: Characterization of the metal-ion binding site of the enzyme from pig allantoic fluid. Biochemical and Biophysical Research Communications, 94 2: 600-605. doi:10.1016/0006-291X(80)91274-7


Author Keough D.T.
Dionysius D.A.
de Jersey J.
Zerner B.
Title Iron-containing acid phosphatases: Characterization of the metal-ion binding site of the enzyme from pig allantoic fluid
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 1090-2104
Publication date 1980-05-30
Sub-type Article (original research)
DOI 10.1016/0006-291X(80)91274-7
Volume 94
Issue 2
Start page 600
End page 605
Total pages 6
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract All of the iron can be removed from the violet acid phosphatase of pig allantoic fluid by treatment with sodium dithionite at pH 4.9. Of the two moles of iron present per mole of enzyme (40,000 g), half is lost rapidly, and the remainder much more slowly. Removal of half of the iron causes complete loss of acid phosphatase activity. Conditions have been defined for the isolation and complete reconstitution [by Fe(II) and β-mercaptoethanol] of two apoenzymes, designated "iron-free" and "one-iron" apoenzymes. Zn2+ ions restore most of the acid phosphatase activity to the one-iron apoenzyme but not to the iron-free enzyme. No metal ions other than Fe(II) and Fe(III) restore significant activity to the iron-free apoenzyme, but Zn(II) and Ni(II) bind tightly to it.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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Created: Tue, 23 Aug 2016, 14:06:45 EST by System User