The interaction of phosphate with the purple acid phosphatase from beef spleen: evidence that phosphate binding is accompanied by oxidation of the iron chromophore.

Abstract:

:Reaction of the reduced (pink) form of the purple acid phosphatase from beef spleen with excess phosphate at pH 5.0, monitored by optical and low temperature EPR spectroscopy and by measurement of enzymatic activity, results in parallel loss of activity and oxidation of the iron chromophore. Colorimetric and radiochemical (32P) experiments indicate the presence of one mole of tightly bound phosphate in the oxidized (purple) form of the enzyme; this phosphate is released upon reduction. Acid hydrolysis of 32P-phosphate-containing enzyme, followed by high voltage paper electrophoresis, gave no evidence for significant amounts of acid-stable phosphoamino acids.

authors

Burman S,Davis JC,Weber MJ,Averill BA

doi

10.1016/0006-291x(86)90467-5

subject

Has Abstract

pub_date

1986-04-29 00:00:00

pages

490-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(86)90467-5

journal_volume

136

pub_type

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