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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Published in | Clinica chimica acta Vol. 120; no. 1; pp. 29 - 40 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
26.03.1982
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Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0009-8981 1873-3492 |
DOI: | 10.1016/0009-8981(82)90074-2 |