Iron-containing acid phosphatases: Interaction of phosphate with the enzyme from pig allantoic fluid

Keough D.T., Beck J.L., de Jersey J. and Zerner B. (1982) Iron-containing acid phosphatases: Interaction of phosphate with the enzyme from pig allantoic fluid. Biochemical and Biophysical Research Communications, 108 4: 1643-1648. doi:10.1016/S0006-291X(82)80098-3


Author Keough D.T.
Beck J.L.
de Jersey J.
Zerner B.
Title Iron-containing acid phosphatases: Interaction of phosphate with the enzyme from pig allantoic fluid
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 1090-2104
Publication date 1982-10-29
Sub-type Article (original research)
DOI 10.1016/S0006-291X(82)80098-3
Open Access Status Not Open Access
Volume 108
Issue 4
Start page 1643
End page 1648
Total pages 6
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract Phosphate binds to the reduced, catalytically active form of pig allantoic fluid acid phosphatase (λmax = 510 nm) at pH 4.9, causing a very rapid spectral shift to a λmax of 540 nm. This spectral shift has permitted the determination of a Kd value of ∼6mM for phosphate binding to the reduced enzyme. Phosphate also greatly potentiates the conversion of the reduced form of the enzyme to a violet, catalytically inactive form. [32P] Phosphate was used to show that phosphate is bound very tightly in this violet form of the enzyme, in a 1:1 complex. The tightly bound phosphate may be removed by reduction of the enzyme or by treatment with 6 M guanidinium chloride. Some previous studies on iron-containing acid phosphatases may well have been complicated by the presence of variable amounts of tightly bound phosphate.
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, 28 Jun 2016, 15:13:01 EST by System User