| dc.contributor |
Departments of Pediatrics and Neurology, Section of Pediatric Neurology, University of Michigan Medical Center, Ann Arbor, MI 48109, USA |
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| dc.contributor |
Department of Human Genetics and Department of Pediatrics, Children's Medical Center, Medical College of Virginia, Richmond, VA 23298, USA |
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| dc.contributor |
Department of Human Genetics and Department of Pediatrics, Children's Medical Center, Medical College of Virginia, Richmond, VA 23298, USA |
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| dc.contributor |
Department of Pediatrics, University of Colorado School of Medicine, Denver, CO 80262, USA |
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| dc.contributor |
Departments of Pediatrics and Biochemistry, Medical College of Wisconsin and the Milwaukee Children's Hospital, Milwaukee, WI5 3233, USA |
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| dc.creator |
Wolf, Barry |
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| dc.creator |
Grier, Robert E. |
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| dc.creator |
Allen, Richard J. |
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| dc.creator |
Goodman, Stephen I. |
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| dc.creator |
Kien, Craig L. |
|
| dc.date |
2006-04-07T18:40:25Z |
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| dc.date |
2006-04-07T18:40:25Z |
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| dc.date |
1983-07-15 |
|
| dc.date.accessioned |
2022-05-19T13:29:53Z |
|
| dc.date.available |
2022-05-19T13:29:53Z |
|
| dc.identifier |
Wolf, Barry, Grier, Robert E., Allen, Richard J., Goodman, Stephen I., Kien, Craig L. (1983/07/15)."Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency." Clinica Chimica Acta 131(3): 273-281. <http://hdl.handle.net/2027.42/25162> |
|
| dc.identifier |
http://www.sciencedirect.com/science/article/B6T57-47P90K9-MH/2/f25d685ec37e256bd1e199fa5cb4ce3e |
|
| dc.identifier |
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6883721&dopt=citation |
|
| dc.identifier |
http://hdl.handle.net/2027.42/25162 |
|
| dc.identifier |
6883721 |
|
| dc.identifier |
http://dx.doi.org/10.1016/0009-8981(83)90096-7 |
|
| dc.identifier |
Clinica Chimica Acta |
|
| dc.identifier.uri |
http://localhost:8080/xmlui/handle/CUHPOERS/117300 |
|
| dc.description |
Late-onset multiple carboxylase deficiency is characterized clinically by skin rash, alopecia, seizures and ataxia and occasionally by candidiasis and developmental delay. Biochemically, these individuals exhibit findings consistent with a combined deficiency of the biotin-dependent carboxylases. We have found that the activity of the enzyme biotinidase is also deficient in the sera of five affected children (0 to 3% of mean control activity, 5.80 +/- 0.89 nmol [middle dot] min- [middle dot] ml- serum), and believe that it represents the primary biochemical defect in this disease. Biotinidase catalyzes the removal of biotin from the [epsilon]-amino group of lysine, through which biotin is covalently bound to the four known human carboxylases, thereby regenerating biotin for reutilization. The deficient activity in our patients was not due to an inhibitor, particularly biotin. It is also not a consequence of feedback control in affected individuals under treatment with pharmacologie doses of biotin. The biotinidase activities of the parents of those children who were available for study were intermediate between deficient and normal values (46% to 65% of mean normal activity). Children lacking biotinidase activity are unable to recycle biotin, and are thus entirely dependent upon exogenous biotin to prevent deficiency. Our findings indicate that the primary biochemical defect in late-onset multiple carboxylase deficiency is in biotinidase activity which is inherited as an autosomal recessive trait. |
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| dc.description |
Peer Reviewed |
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| dc.description |
http://deepblue.lib.umich.edu/bitstream/2027.42/25162/1/0000598.pdf |
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| dc.format |
767250 bytes |
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| dc.format |
3118 bytes |
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| dc.format |
application/pdf |
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| dc.format |
text/plain |
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| dc.format |
application/pdf |
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| dc.language |
en_US |
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| dc.publisher |
Elsevier |
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| dc.rights |
IndexNoFollow |
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| dc.subject |
Pathology |
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| dc.subject |
Health Sciences |
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| dc.title |
Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency |
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| dc.type |
Article |
|