Dehydrogenase-modified carbon-fiber microelectrodes for the measurement of neurotransmitter dynamics. 2. Covalent modification utilizing avidin-biotin technology
Dehydrogenase enzymes are immobilized onto carbon-fiber microelectrode surfaces via avidin-biotin technology and a covalently linked hydrophilic tether. The avidin-biotin coupling strategy allows the selectivity of the electrochemical measurement to be easily changed without reoptimizing the immobil...
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| Veröffentlicht in: | Analytical chemistry (Washington) 1993-03, Vol.65 (5), p.623-630 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Pantano, Paul Kuhr, Werner G |
| description | Dehydrogenase enzymes are immobilized onto carbon-fiber microelectrode surfaces via avidin-biotin technology and a covalently linked hydrophilic tether. The avidin-biotin coupling strategy allows the selectivity of the electrochemical measurement to be easily changed without reoptimizing the immobilization conditions. Optimized derivatization conditions are demonstrated for dimer, tetramer, and hexamer dehydrogenases. Nonelectroactive substrates (ethanol, glucose-6-phosphate, and glutamate) are quantitated through the detection of enzyme-generated NADH by fast scan cyclic staircase voltammetry (100 V/s). The glutamate dehydrogenase-modified microelectrode possesses a 300-ms response time with a detection limit of 0.5 mM glutamate and a 1-60 mM linear concentration range. |
| doi_str_mv | 10.1021/ac00053a023 |
| format | Article |
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The glutamate dehydrogenase-modified microelectrode possesses a 300-ms response time with a detection limit of 0.5 mM glutamate and a 1-60 mM linear concentration range.</description><subject>Avidin - chemistry</subject><subject>Biochemistry</subject><subject>Biosensing Techniques</subject><subject>Biotin - chemistry</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized</subject><subject>Glutamate Dehydrogenase - metabolism</subject><subject>Glutamates - analysis</subject><subject>Microelectrodes</subject><subject>Neurotransmitter Agents - analysis</subject><subject>Polymers</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkUFv1DAQhSMEKkvhxBnJ4gAHlGXsxHFyhIUCUlcgUc6W44x3XRK7tZ2K5d_wT3GVVUGIkyW_780bzSuKpxTWFBh9rTQA8EoBq-4VK8oZlE3bsvvFKv9XJRMAD4tHMV4CUAq0OSlOWui4EO2q-PUO94ch-B06FbGc_GCNxYFoFXrvSmN7DGSyOngcUafgB4zE-EDSHsmEKs4BJ3SJeEMczsGnoFycbErZNxycyt64JmxNNv5GjbfkkqFVst6ROdnR_rRuR9SNHawre-uTdSSh3js_-t3hcfHAqDHik-N7Wnw7e3-x-Vief_7wafPmvFR1LVLZaWRtb6DiVBjOug64qbhueasoiJpBbQRQHASjPddcNKLhjLemzQaqh7o6LV4sc6-Cv54xJjnZqHEclUM_Ryl4Q5u66zL4_B_w0s_B5d0koyIHsopm6NUC5cvFGNDIq2AnFQ6SgrxtTf7VWqafHUfO_YTDHXusKevlotuY8MedrMJ32YhKcHnx5as8Y1vYVrCVbzP_cuGVjn-2-1_yb8kAr9Q</recordid><startdate>19930301</startdate><enddate>19930301</enddate><creator>Pantano, Paul</creator><creator>Kuhr, Werner G</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19930301</creationdate><title>Dehydrogenase-modified carbon-fiber microelectrodes for the measurement of neurotransmitter dynamics. 2. 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Covalent modification utilizing avidin-biotin technology</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>1993-03-01</date><risdate>1993</risdate><volume>65</volume><issue>5</issue><spage>623</spage><epage>630</epage><pages>623-630</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Dehydrogenase enzymes are immobilized onto carbon-fiber microelectrode surfaces via avidin-biotin technology and a covalently linked hydrophilic tether. The avidin-biotin coupling strategy allows the selectivity of the electrochemical measurement to be easily changed without reoptimizing the immobilization conditions. Optimized derivatization conditions are demonstrated for dimer, tetramer, and hexamer dehydrogenases. Nonelectroactive substrates (ethanol, glucose-6-phosphate, and glutamate) are quantitated through the detection of enzyme-generated NADH by fast scan cyclic staircase voltammetry (100 V/s). The glutamate dehydrogenase-modified microelectrode possesses a 300-ms response time with a detection limit of 0.5 mM glutamate and a 1-60 mM linear concentration range.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>8095778</pmid><doi>10.1021/ac00053a023</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2700 |
| ispartof | Analytical chemistry (Washington), 1993-03, Vol.65 (5), p.623-630 |
| issn | 0003-2700 1520-6882 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Avidin - chemistry Biochemistry Biosensing Techniques Biotin - chemistry Enzymes Enzymes, Immobilized Glutamate Dehydrogenase - metabolism Glutamates - analysis Microelectrodes Neurotransmitter Agents - analysis Polymers |
| title | Dehydrogenase-modified carbon-fiber microelectrodes for the measurement of neurotransmitter dynamics. 2. Covalent modification utilizing avidin-biotin technology |
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