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1 one H4 were biotinylated enzymatically using biotinidase.
2 described enzymatic activities of the enzyme biotinidase.
5 n of histones, mRNA encoding biotinidase and biotinidase activity did not parallel the increased biot
6 e analytical method for the determination of biotinidase activity using the blood sample deposited on
8 lysis activity that is distinct from that of biotinidase and bile salt-stimulated lipase in lymphobla
9 in biotinylation of histones, mRNA encoding biotinidase and biotinidase activity did not parallel th
11 of histone H4 were effectively recognized by biotinidase as substrates for biotinylation; in contrast
16 nsertion mutation within exon D of the human biotinidase gene in a child with biotinidase deficiency.
18 identified a novel point mutation within the biotinidase gene that encodes the signal peptide in two
19 old boy with biotin dependency not caused by biotinidase, holocarboxylase synthetase, or nutritional
23 nes might be regulated by enzymes other than biotinidase or by the rate of histone debiotinylation.
25 80 and Vanin-1 are 40% homologous with human biotinidase suggests the existence of a biotinidase supe
26 uman biotinidase suggests the existence of a biotinidase superfamily of molecules that may be involve
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