| pubmed-article:73375 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0004002 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0332157 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
| pubmed-article:73375 | lifeskim:mentions | umls-concept:C0947682 | lld:lifeskim |
| pubmed-article:73375 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:73375 | pubmed:dateCreated | 1978-1-27 | lld:pubmed |
| pubmed-article:73375 | pubmed:abstractText | Mercurochrome strongly inhibits aspartate transaminase and 2,3-dicarboxyethylated aspartate transaminase. The native enzyme exhibits a biphasic time-course of inactivation by mercurochrome with second-order rate constants 1.62 x 10(4) M-1 - min-1 and 2.15 x 10(3) M-1 - min-1, whereas the modified enzyme is inactivated more slowly (second-order rate constant 6.1 x 10(2) M-1 - min-1) under the same conditions. The inhibitor inactivates native and modified enzyme in the absence as well as in the presence of substrates. Mercurochrome-transaminase interaction is accompanied by a red shift in the absorption maximum of the fluorochrome of about 10 nm. Difference spectra of the mercurochrome-enzyme system versus mercurochrome, compared with analogous spectra of mercurochrome-ethanol, revealed that the spectral shifts recorded during mercurochrome-transaminase interaction are similar to those that occur when mercurochrome is dissolved in non-polar solvents. Studies of mercurochrome complexes with native or modified transaminase, isolated by chromatography on Sephadex G-25, revealed that native transaminase is able to conjugate with four mercurochrome molecules per molecule, but the modified enzyme is able to conjugate with only two mercurochrome molecules per molecule. | lld:pubmed |
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| pubmed-article:73375 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:73375 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:73375 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:73375 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:73375 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:73375 | pubmed:author | pubmed-author:Evangelopoulo... | lld:pubmed |
| pubmed-article:73375 | pubmed:author | pubmed-author:KalogerakosT... | lld:pubmed |
| pubmed-article:73375 | pubmed:author | pubmed-author:Dimitropoulos... | lld:pubmed |
| pubmed-article:73375 | pubmed:author | pubmed-author:OikonomakosN... | lld:pubmed |
| pubmed-article:73375 | pubmed:author | pubmed-author:Karni-katsadi... | lld:pubmed |
| pubmed-article:73375 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:73375 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:73375 | pubmed:volume | 167 | lld:pubmed |
| pubmed-article:73375 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:73375 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:73375 | pubmed:pagination | 53-63 | lld:pubmed |
| pubmed-article:73375 | pubmed:dateRevised | 2010-9-1 | lld:pubmed |
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| pubmed-article:73375 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:73375 | pubmed:articleTitle | Interaction of aspartate aminotransferase with mercurochrome. Relationship of an exposed thiol group of the enzyme to the active centre. | lld:pubmed |
| pubmed-article:73375 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:73375 | lld:pubmed |
