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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Burman S,Davis JC,Weber MJ,Averill BAdoi
10.1016/0006-291x(86)90467-5subject
Has Abstractpub_date
1986-04-29 00:00:00pages
490-7issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(86)90467-5journal_volume
136pub_type
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