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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1984-1-7
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pubmed:abstractText |
Estradiol 17 beta-dehydrogenase of human placenta was rapidly inactivated by 2,3-butanedione under u.v. light, and no protection against the inactivation was observed in the presence of sodium azide. Under ordinary laboratory illumination, the inactivation was biphasically progressed in time-dependent and concentration-dependent manners, while a partial protection from the inactivation was indicated by sodium azide. These results suggest that the inactivation mechanism of the dehydrogenase by 2,3-butanedione under laboratory illumination is different from that under u.v. light. Therefore, the inactivation under laboratory illumination proceeded by a reaction with excited singlet molecular oxygen (1 delta g or 1 sigma +g states), and that under u.v. light was caused by a reaction of substrate with triplet sensitizer. In the presence of NADP+, the inactivation of the enzyme by 2,3-butanedione was markedly reduced. The maximum protection by NADP+ was about 80% of the initial enzyme activity. Amino acid analysis of the enzyme treated with 2,3-butanedione under laboratory illumination showed that the modified enzyme contained considerably less of the following amino acids than the native enzyme: histidine, arginine, threonine, methionine, tyrosine and leucine. In addition, other dicarbonyl reagents, 1,4-dibromo-2,3-butanedione, 1-phenyl-1,2-propanedione, phenylglyoxal, 16-oxoestrone, 1,2-cyclohexanedione, 2,4-pentanedione and glyoxal were found to decrease the dehydrogenase activity in various degree.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/17-Hydroxysteroid Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Butanones,
http://linkedlifedata.com/resource/pubmed/chemical/Diacetyl,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol Dehydrogenases
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-4731
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1617-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6580513-17-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:6580513-Amino Acids,
pubmed-meshheading:6580513-Butanones,
pubmed-meshheading:6580513-Diacetyl,
pubmed-meshheading:6580513-Estradiol Dehydrogenases,
pubmed-meshheading:6580513-Female,
pubmed-meshheading:6580513-Humans,
pubmed-meshheading:6580513-Hydrogen-Ion Concentration,
pubmed-meshheading:6580513-Kinetics,
pubmed-meshheading:6580513-Photolysis,
pubmed-meshheading:6580513-Placenta,
pubmed-meshheading:6580513-Pregnancy,
pubmed-meshheading:6580513-Structure-Activity Relationship
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pubmed:year |
1983
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pubmed:articleTitle |
Photochemical inactivation of human placental estradiol 17 beta-dehydrogenase in the presence of 2,3-butanedione.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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