Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1978-1-27
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-1164432, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-13610891, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-13650640, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-14284115, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-14417169, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-14449825, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-14907689, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-236186, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-4358818, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-4673054, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-4694734, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-4795364, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-4795558, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-4797900, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-5065588, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-5432, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-5529033, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-5781269, http://linkedlifedata.com/resource/pubmed/commentcorrection/73375-6024760
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
167
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
53-63
pubmed:dateRevised
2010-9-1
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Interaction of aspartate aminotransferase with mercurochrome. Relationship of an exposed thiol group of the enzyme to the active centre.
pubmed:publicationType
Journal Article