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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1989-3-17
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pubmed:abstractText |
Biotinidase shows two binding sites for biotin, with Kd = 59 and 3 nM respectively, and requires tryptophan and cysteine residues of the biotinidase protein for biotin-binding activity. Analysis of human serum by various column-chromatographic techniques indicates that biotinidase is the only protein which exchanges with labelled (+)-biotin. It was shown previously that epileptic patients receiving a high average dose of anticonvulsants (containing a carbamide group) have lower biotin concentrations than those receiving a low dose. We have shown in human serum and with purified biotinidase that these anticonvulsant drugs compete with biotin for binding to the protein moiety.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-13767412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-13901438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-14101981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-14161000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-14217155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-14311756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3107856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3111297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3122856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3593216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3860169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3860178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3925856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3925858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3925859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3925986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3930842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3949811,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-3951999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-4553496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-5319359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-5354931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-5354932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-5528638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-567647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-5969276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-6129246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-6129846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-6476376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-6539128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-6828095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-6883721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-7073724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-7251693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223902-962874
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Biotin,
http://linkedlifedata.com/resource/pubmed/chemical/Biotinidase,
http://linkedlifedata.com/resource/pubmed/chemical/Bromosuccinimide,
http://linkedlifedata.com/resource/pubmed/chemical/Carbamazepine,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloromercuribenzoates,
http://linkedlifedata.com/resource/pubmed/chemical/Globulins,
http://linkedlifedata.com/resource/pubmed/chemical/Phenobarbital,
http://linkedlifedata.com/resource/pubmed/chemical/Phenytoin,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/biotin-binding proteins,
http://linkedlifedata.com/resource/pubmed/chemical/p-Chloromercuribenzoic Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
256
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-70
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3223902-Amidohydrolases,
pubmed-meshheading:3223902-Binding Sites,
pubmed-meshheading:3223902-Biotin,
pubmed-meshheading:3223902-Biotinidase,
pubmed-meshheading:3223902-Bromosuccinimide,
pubmed-meshheading:3223902-Carbamazepine,
pubmed-meshheading:3223902-Carrier Proteins,
pubmed-meshheading:3223902-Centrifugation, Density Gradient,
pubmed-meshheading:3223902-Chloromercuribenzoates,
pubmed-meshheading:3223902-Chromatography, Gel,
pubmed-meshheading:3223902-Globulins,
pubmed-meshheading:3223902-Humans,
pubmed-meshheading:3223902-Hydrogen-Ion Concentration,
pubmed-meshheading:3223902-Phenobarbital,
pubmed-meshheading:3223902-Phenytoin,
pubmed-meshheading:3223902-Serum Albumin,
pubmed-meshheading:3223902-p-Chloromercuribenzoic Acid
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pubmed:year |
1988
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pubmed:articleTitle |
Role of human serum biotinidase as biotin-binding protein.
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pubmed:affiliation |
Department of Biochemistry, Faculty of Medicine, University of Manitoba, Winnipeg, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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