pubmed-article:19362208 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C0018026 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C0041942 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C0041945 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C0600364 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C0032474 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C1450054 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C0013812 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C1705938 | lld:lifeskim |
pubmed-article:19362208 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:19362208 | pubmed:issue | 4-5 | lld:pubmed |
pubmed-article:19362208 | pubmed:dateCreated | 2009-4-13 | lld:pubmed |
pubmed-article:19362208 | pubmed:abstractText | An amperometric biosensor was fabricated for the quantitative determination of urea in aqueous medium using hematein, a pH-sensitive natural dye. The urease (Urs) was covalently immobilized onto an electrode made of gold nanoparticles functionalized with hyperbranched polyester-Boltron H40 (H40-Au) coated onto an indium-tin oxide (ITO) covered glass substrate. The covalent linkage between the Urs enzyme and H40-Au nanoparticles provided the resulting enzyme electrode (Urs/H40-Au/ITO) with a high level of enzyme immobilization and excellent lifetime stability. The response studies were carried out as a function of urea concentration with amperometric and photometric measurements. The biosensor based on Urs/H40-Au/ITO as the working electrode showed a linear current response to the urea concentration ranging from 0.01 to 35 mM. The urea biosensor exhibited a sensitivity of 7.48 nA/mM with a response time of 3s. The Michaelis-Menten constant for the Urs/H40-Au/ITO biosensor was calculated to be 0.96 mM, indicating the Urs enzyme immobilized on the electrode surface had a high affinity to urea. | lld:pubmed |
pubmed-article:19362208 | pubmed:language | eng | lld:pubmed |
pubmed-article:19362208 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19362208 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19362208 | pubmed:month | Jun | lld:pubmed |
pubmed-article:19362208 | pubmed:issn | 1873-3573 | lld:pubmed |
pubmed-article:19362208 | pubmed:author | pubmed-author:TiwariAshutos... | lld:pubmed |
pubmed-article:19362208 | pubmed:author | pubmed-author:AryalSantoshS | lld:pubmed |
pubmed-article:19362208 | pubmed:author | pubmed-author:GongShaoqinS | lld:pubmed |
pubmed-article:19362208 | pubmed:author | pubmed-author:PillaSrikanth... | lld:pubmed |
pubmed-article:19362208 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19362208 | pubmed:day | 15 | lld:pubmed |
pubmed-article:19362208 | pubmed:volume | 78 | lld:pubmed |
pubmed-article:19362208 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19362208 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19362208 | pubmed:pagination | 1401-7 | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:meshHeading | pubmed-meshheading:19362208... | lld:pubmed |
pubmed-article:19362208 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19362208 | pubmed:articleTitle | An amperometric urea biosensor based on covalently immobilized urease on an electrode made of hyperbranched polyester functionalized gold nanoparticles. | lld:pubmed |
pubmed-article:19362208 | pubmed:affiliation | Department of Mechanical Engineering, University of Wisconsin-Milwaukee, 3200 North Cramer Street, Milwaukee, WI 53211, USA. | lld:pubmed |
pubmed-article:19362208 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19362208 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:19362208 | pubmed:publicationType | Evaluation Studies | lld:pubmed |