Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases / blood*
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Binding Sites
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Biotin / metabolism*
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Biotinidase
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Bromosuccinimide / pharmacology
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Carbamazepine / pharmacology
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Carrier Proteins / metabolism*
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Centrifugation, Density Gradient
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Chloromercuribenzoates / pharmacology
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Chromatography, Gel
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Globulins / metabolism
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Humans
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Hydrogen-Ion Concentration
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Phenobarbital / pharmacology
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Phenytoin / pharmacology
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Serum Albumin / metabolism
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p-Chloromercuribenzoic Acid
Substances
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Carrier Proteins
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Chloromercuribenzoates
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Globulins
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Serum Albumin
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biotin-binding proteins
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Carbamazepine
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p-Chloromercuribenzoic Acid
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Phenytoin
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Biotin
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Amidohydrolases
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Biotinidase
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Bromosuccinimide
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Phenobarbital