| pubmed-article:18514640 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18514640 | lifeskim:mentions | umls-concept:C0085281 | lld:lifeskim |
| pubmed-article:18514640 | lifeskim:mentions | umls-concept:C0009170 | lld:lifeskim |
| pubmed-article:18514640 | lifeskim:mentions | umls-concept:C0600688 | lld:lifeskim |
| pubmed-article:18514640 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:18514640 | lifeskim:mentions | umls-concept:C0201734 | lld:lifeskim |
| pubmed-article:18514640 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:18514640 | pubmed:issue | 1-3 | lld:pubmed |
| pubmed-article:18514640 | pubmed:dateCreated | 2008-9-8 | lld:pubmed |
| pubmed-article:18514640 | pubmed:abstractText | Butyrylcholinesterase (BChE, EC 3.1.1.8) is important in human cocaine metabolism despite its limited ability to hydrolyze this drug. Efforts to improve the catalytic efficiency of this enzyme have led to a quadruple mutant cocaine hydrolase, "CocH", that in animal models of addiction appears promising for treatment of overdose and relapse. We incorporated the CocH mutations into a BChE-albumin fusion protein, "Albu-CocH", and evaluated the pharmacokinetics of the enzyme after i.v. injection in rats. As assessed from the time course of cocaine hydrolyzing activity in plasma, Albu-CocH redistributed into extracellular fluid (16% of estimated total body water) with a t(1/2) of 0.66h and it underwent elimination with a t(1/2) of 8h. These results indicate that the enzyme has ample stability for short-term applications and may be suitable for longer-term treatment as well. Present data also confirm the markedly enhanced power of Albu-CocH for cocaine hydrolysis and they support the view that Albu-CocH might prove valuable in treating phenomena associated with cocaine abuse. | lld:pubmed |
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| pubmed-article:18514640 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18514640 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18514640 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18514640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18514640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18514640 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18514640 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:18514640 | pubmed:issn | 0009-2797 | lld:pubmed |
| pubmed-article:18514640 | pubmed:author | pubmed-author:GaoYangY | lld:pubmed |
| pubmed-article:18514640 | pubmed:author | pubmed-author:BrimijoinStep... | lld:pubmed |
| pubmed-article:18514640 | pubmed:author | pubmed-author:ZhaoQinghaiQ | lld:pubmed |
| pubmed-article:18514640 | pubmed:author | pubmed-author:SinghMallikaM | lld:pubmed |
| pubmed-article:18514640 | pubmed:author | pubmed-author:ShahRutulR | lld:pubmed |
| pubmed-article:18514640 | pubmed:author | pubmed-author:LaFleurDavidD | lld:pubmed |
| pubmed-article:18514640 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18514640 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:18514640 | pubmed:volume | 175 | lld:pubmed |
| pubmed-article:18514640 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18514640 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18514640 | pubmed:pagination | 83-7 | lld:pubmed |
| pubmed-article:18514640 | pubmed:dateRevised | 2011-5-13 | lld:pubmed |
| pubmed-article:18514640 | pubmed:meshHeading | pubmed-meshheading:18514640... | lld:pubmed |
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| pubmed-article:18514640 | pubmed:meshHeading | pubmed-meshheading:18514640... | lld:pubmed |
| pubmed-article:18514640 | pubmed:meshHeading | pubmed-meshheading:18514640... | lld:pubmed |
| pubmed-article:18514640 | pubmed:meshHeading | pubmed-meshheading:18514640... | lld:pubmed |
| pubmed-article:18514640 | pubmed:meshHeading | pubmed-meshheading:18514640... | lld:pubmed |
| pubmed-article:18514640 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18514640 | pubmed:articleTitle | An albumin-butyrylcholinesterase for cocaine toxicity and addiction: catalytic and pharmacokinetic properties. | lld:pubmed |
| pubmed-article:18514640 | pubmed:affiliation | Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, 200 First Street SW, Rochester, MN 55905, USA. | lld:pubmed |
| pubmed-article:18514640 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18514640 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18514640 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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