Evaluation of the fluorometric protein phosphatase inhibition assay in the determination of okadaic acid in mussels
The protein phosphatase inhibition assay for okadaic acid, the major DSP toxin, modified to use the fluorescence substrates methylumbelliferyl phosphate (MUP) and fluorescein diphosphate (FDP), was compared to the assay using p-nitrophenylphosphate ( p-NPP) and the bioluminescence assay using lucife...
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| Veröffentlicht in: | Toxicon (Oxford) 1999-06, Vol.37 (6), p.909-922 |
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| creator | Mountfort, Douglas O Kennedy, Glenn Garthwaite, Ian Michael Quilliam Truman, Pennelope Hannah, Donald J |
| description | The protein phosphatase inhibition assay for okadaic acid, the major DSP toxin, modified to use the fluorescence substrates methylumbelliferyl phosphate (MUP) and fluorescein diphosphate (FDP), was compared to the assay using
p-nitrophenylphosphate (
p-NPP) and the bioluminescence assay using luciferin phosphate (L–P). Under the standard assay conditions used okadaic acid inhibited the enzyme activity dose-dependently with IC
50 values of 1.5 nM (MUP) and 1.2 nM (FDP). This compares to IC
50 values of 0.9 and 6 nM using L–P and
p-NPP respectively. CDP-
star, a chemiluminescence substrate, was not hydrolysed by the enzyme. Decreasing the enzyme concentration lowered the IC
50 for the colorimetric method (IC
50=2 nM [
p-NPP], 0.75 nM enzyme) but no shift was observed with fluorimetry. However at enzyme concentrations ELISA>PP-2A>LC–MS. The fluorimetric assay was both more sensitive and accurate than the colorimetric assay (the latter showed a propensity towards false positives in the region 20 μg/100 g), and the moderate increase in equipment cost appears to be outweighed by the performance of the method. |
| doi_str_mv | 10.1016/S0041-0101(98)00222-0 |
| format | Article |
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p-nitrophenylphosphate (
p-NPP) and the bioluminescence assay using luciferin phosphate (L–P). Under the standard assay conditions used okadaic acid inhibited the enzyme activity dose-dependently with IC
50 values of 1.5 nM (MUP) and 1.2 nM (FDP). This compares to IC
50 values of 0.9 and 6 nM using L–P and
p-NPP respectively. CDP-
star, a chemiluminescence substrate, was not hydrolysed by the enzyme. Decreasing the enzyme concentration lowered the IC
50 for the colorimetric method (IC
50=2 nM [
p-NPP], 0.75 nM enzyme) but no shift was observed with fluorimetry. However at enzyme concentrations <1.5 nM (standard assay) the error margin was too great for routine analysis. The method using fluorimetry allowed detection of okadaic acid concentrations to levels ≤1 μg/100 g of mussel tissue which is well below the limit of 20 μg/100 g (mouse bioassay) set by some regulatory agencies. Determination of the toxin content in naturally contaminated mussels in three separate experiments gave coefficients of variance ranging from 16 to 29% (MUP) and from 8 to 78% (
p-NPP). Multicomparison studies showed that concentrations of okadaic acid in naturally contaminated mussel samples determined by fluorescence generally agreed with those obtained using ELISA and LC–MS procedures, and with the mouse bioassay. However using the mouse bioassay as the standard, values determined by the ELISA, PP-2A and LC–MS all scored false negative results compared to those for the mouse bioassay in the range 20–40 μg/100 g mussel, and at the limit of the mouse bioassay the values by the other three methods were substantially less. With few exceptions the methods scored okadaic acid with highest to lowest values in the following order: mouse bioassay>ELISA>PP-2A>LC–MS. The fluorimetric assay was both more sensitive and accurate than the colorimetric assay (the latter showed a propensity towards false positives in the region 20 μg/100 g), and the moderate increase in equipment cost appears to be outweighed by the performance of the method.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/S0041-0101(98)00222-0</identifier><identifier>PMID: 10340830</identifier><identifier>CODEN: TOXIA6</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Animals ; assays ; Biological and medical sciences ; Bivalvia - chemistry ; Bivalvia - enzymology ; colorimetry ; comparisons ; contamination ; derivatives ; Dose-Response Relationship, Drug ; enzyme activity ; Enzyme-Linked Immunosorbent Assay ; fluorescein ; fluorescein diphosphate ; fluorimetry ; Fluorometry - methods ; inhibition ; Injections, Intraperitoneal ; Lipids - administration & dosage ; Lipids - toxicity ; Luminescent Measurements ; Medical sciences ; methylumbelliferyl phosphate ; Mice ; Mollusca ; mussels ; Mytilus edulis ; Okadaic Acid - analysis ; Perna canaliculus ; phosphates (esters) ; phosphoprotein phosphatase ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Plant poisons toxicology ; Reproducibility of Results ; Sensitivity and Specificity ; Substrate Specificity ; Tissue Extracts - administration & dosage ; Tissue Extracts - toxicity ; Toxicology ; toxins</subject><ispartof>Toxicon (Oxford), 1999-06, Vol.37 (6), p.909-922</ispartof><rights>1999 Elsevier Science Ltd</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-7eebdb34cb42ef2e9efd3af0eb0822c806e3c062eef715954a2cb15bb1ecc2103</citedby><cites>FETCH-LOGICAL-c511t-7eebdb34cb42ef2e9efd3af0eb0822c806e3c062eef715954a2cb15bb1ecc2103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0041-0101(98)00222-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1775429$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10340830$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mountfort, Douglas O</creatorcontrib><creatorcontrib>Kennedy, Glenn</creatorcontrib><creatorcontrib>Garthwaite, Ian</creatorcontrib><creatorcontrib>Michael Quilliam</creatorcontrib><creatorcontrib>Truman, Pennelope</creatorcontrib><creatorcontrib>Hannah, Donald J</creatorcontrib><title>Evaluation of the fluorometric protein phosphatase inhibition assay in the determination of okadaic acid in mussels</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>The protein phosphatase inhibition assay for okadaic acid, the major DSP toxin, modified to use the fluorescence substrates methylumbelliferyl phosphate (MUP) and fluorescein diphosphate (FDP), was compared to the assay using
p-nitrophenylphosphate (
p-NPP) and the bioluminescence assay using luciferin phosphate (L–P). Under the standard assay conditions used okadaic acid inhibited the enzyme activity dose-dependently with IC
50 values of 1.5 nM (MUP) and 1.2 nM (FDP). This compares to IC
50 values of 0.9 and 6 nM using L–P and
p-NPP respectively. CDP-
star, a chemiluminescence substrate, was not hydrolysed by the enzyme. Decreasing the enzyme concentration lowered the IC
50 for the colorimetric method (IC
50=2 nM [
p-NPP], 0.75 nM enzyme) but no shift was observed with fluorimetry. However at enzyme concentrations <1.5 nM (standard assay) the error margin was too great for routine analysis. The method using fluorimetry allowed detection of okadaic acid concentrations to levels ≤1 μg/100 g of mussel tissue which is well below the limit of 20 μg/100 g (mouse bioassay) set by some regulatory agencies. Determination of the toxin content in naturally contaminated mussels in three separate experiments gave coefficients of variance ranging from 16 to 29% (MUP) and from 8 to 78% (
p-NPP). Multicomparison studies showed that concentrations of okadaic acid in naturally contaminated mussel samples determined by fluorescence generally agreed with those obtained using ELISA and LC–MS procedures, and with the mouse bioassay. However using the mouse bioassay as the standard, values determined by the ELISA, PP-2A and LC–MS all scored false negative results compared to those for the mouse bioassay in the range 20–40 μg/100 g mussel, and at the limit of the mouse bioassay the values by the other three methods were substantially less. With few exceptions the methods scored okadaic acid with highest to lowest values in the following order: mouse bioassay>ELISA>PP-2A>LC–MS. 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p-nitrophenylphosphate (
p-NPP) and the bioluminescence assay using luciferin phosphate (L–P). Under the standard assay conditions used okadaic acid inhibited the enzyme activity dose-dependently with IC
50 values of 1.5 nM (MUP) and 1.2 nM (FDP). This compares to IC
50 values of 0.9 and 6 nM using L–P and
p-NPP respectively. CDP-
star, a chemiluminescence substrate, was not hydrolysed by the enzyme. Decreasing the enzyme concentration lowered the IC
50 for the colorimetric method (IC
50=2 nM [
p-NPP], 0.75 nM enzyme) but no shift was observed with fluorimetry. However at enzyme concentrations <1.5 nM (standard assay) the error margin was too great for routine analysis. The method using fluorimetry allowed detection of okadaic acid concentrations to levels ≤1 μg/100 g of mussel tissue which is well below the limit of 20 μg/100 g (mouse bioassay) set by some regulatory agencies. Determination of the toxin content in naturally contaminated mussels in three separate experiments gave coefficients of variance ranging from 16 to 29% (MUP) and from 8 to 78% (
p-NPP). Multicomparison studies showed that concentrations of okadaic acid in naturally contaminated mussel samples determined by fluorescence generally agreed with those obtained using ELISA and LC–MS procedures, and with the mouse bioassay. However using the mouse bioassay as the standard, values determined by the ELISA, PP-2A and LC–MS all scored false negative results compared to those for the mouse bioassay in the range 20–40 μg/100 g mussel, and at the limit of the mouse bioassay the values by the other three methods were substantially less. With few exceptions the methods scored okadaic acid with highest to lowest values in the following order: mouse bioassay>ELISA>PP-2A>LC–MS. The fluorimetric assay was both more sensitive and accurate than the colorimetric assay (the latter showed a propensity towards false positives in the region 20 μg/100 g), and the moderate increase in equipment cost appears to be outweighed by the performance of the method.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>10340830</pmid><doi>10.1016/S0041-0101(98)00222-0</doi><tpages>14</tpages></addata></record> |
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| ispartof | Toxicon (Oxford), 1999-06, Vol.37 (6), p.909-922 |
| issn | 0041-0101 1879-3150 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals assays Biological and medical sciences Bivalvia - chemistry Bivalvia - enzymology colorimetry comparisons contamination derivatives Dose-Response Relationship, Drug enzyme activity Enzyme-Linked Immunosorbent Assay fluorescein fluorescein diphosphate fluorimetry Fluorometry - methods inhibition Injections, Intraperitoneal Lipids - administration & dosage Lipids - toxicity Luminescent Measurements Medical sciences methylumbelliferyl phosphate Mice Mollusca mussels Mytilus edulis Okadaic Acid - analysis Perna canaliculus phosphates (esters) phosphoprotein phosphatase Phosphoprotein Phosphatases - antagonists & inhibitors Plant poisons toxicology Reproducibility of Results Sensitivity and Specificity Substrate Specificity Tissue Extracts - administration & dosage Tissue Extracts - toxicity Toxicology toxins |
| title | Evaluation of the fluorometric protein phosphatase inhibition assay in the determination of okadaic acid in mussels |
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