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Clinical Chemistry, Vol 41, 200-203, Copyright © 1995 by American Association for Clinical Chemistry
S Osawa, S Iida, H Yonemitsu, K Kuroiwa, K Katayama and T Nagasawa
Department of Laboratory Medicine, Chiba University Hospital, Japan.
We characterized six self-indicating substrates, synthesized as the derivative compounds of acetylphenyl phosphate, for serum prostatic acid phosphatase (PAP) activity. One of the substrates, 2,6-dichloro-4- acetylphenyl phosphate (DCAPP), is superior to others in terms of stability, affinity, and low Km for PAP. The hydrolyzed product, 2,6- dichloro-4-acetylphenol (DCAP), has a maximum absorption at 334.2 nm, a pKa of 4.15, and a molar absorptivity at 340 nm of 21,490 L.mol-1.cm-1 in citrate-HCl buffer, pH 5.4. PAP activity was assessed by subtracting tartaric acid-inhibited acid phosphatase activity from total acid phosphatase activity. Our assay system involving DCAPP is a unique kinetic method that shows good reproducibility, wide analytical dynamic range, and high specificity for PAP. Moreover, it is easily adaptable to automated analyzers because the product, DCAP, can be monitored at 340 nm.
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M. Nakanishi, K. Yoh, K. Uchida, S. Maruo, and A. Matsuoka Improved method for measuring tartrate-resistant acid phosphatase activity in serum Clin. Chem., February 1, 1998; 44(2): 221 - 225. [Abstract] [Full Text] [PDF] |
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