Prostatic acid phosphatase, purification and iodination using Iodogen

Prostatic acid phosphatase was purified from prostatic adenomas. The procedure involved chromatography on Concanavalin A-Sepharose, DEAE-cellulose, Bio-Gel P-150 and L-tartrate-Sepharose. The purified phosphatase hydrolyzed p-nitrophenyl phosphate at a rate of 270 μmol · mg −1 min −1 (25°C) and show...

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Bibliographic Details
Published inClinica chimica acta Vol. 120; no. 1; pp. 29 - 40
Main Authors Skinningsrud, Anders, Nustad, Kjell
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 26.03.1982
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Summary:Prostatic acid phosphatase was purified from prostatic adenomas. The procedure involved chromatography on Concanavalin A-Sepharose, DEAE-cellulose, Bio-Gel P-150 and L-tartrate-Sepharose. The purified phosphatase hydrolyzed p-nitrophenyl phosphate at a rate of 270 μmol · mg −1 min −1 (25°C) and showed homogeneity upon polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The final prostatic acid phosphatase preparation was pure and the antisera were monospecific as judged by the highly sensitive technique of crossed immunoelectrophoresis. Of the procedures evaluated for the iodination of the purified enzyme, oxidation with lodogen was found to give the best iodinated product.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0009-8981
1873-3492
DOI:10.1016/0009-8981(82)90074-2