Abstract
Biotinidase [EC 3.5.1.12] catalyzes the removal of biotin from biocytin (ε-N-biotinyl-lysine) or from the ε-amino group of the lysyl residue in partially degraded carboxylases (Thoma and Petersen, 1954). We have recently shown that most individuals with late-onset multiple carboxylase deficiency (MCD) have deficient activity of serum biotinidase by measuring colorimetrically the liberation of p-aminobenzoate from the artificial substrate, N-biotinyl-p-aminobenzoate (Wolf et al., 1983a). We now report the development of a sensitive bioassay for the determination of biotinidase activity using a fibroblast line derived from a patient with a primary deficiency in the activity of holocarboxylase synthetase (Burri et ai, 1981). This enzyme links biotin covalently to the various apoenzymes forming their respective holocarboxylases.
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Burri, B. J., Sweetman, L. and Nyhan, W. L. Mutant holocarboxylase synthetase. Evidence for the enzyme defect in early infantile biotin-responsive multiple carboxylase deficiency. J. Clin. Invest. 68 (1981) 1491–1495
Feldman, G. L., Hsia, Y. E. and Wolf, B. Biochemical characterization of biotin-responsive multiple carboxylase deficiency: Heterogeneity within the bio genetic complementation group. Am. J. Hum. Genet. 33 (1981) 692–701
Pispa, J. Animal biotinidase. Ann. Med. Exp. Biol. Fenn. 43 (1965) 5–39
Thoma, R. M. and Petersen, W. H. The enzymatic degradation of soluble protein bound biotin. J. Biol. Chem. 210 (1954) 569–579
Wolf, B., Grier, R. E., Allen, R. J., Goodman, S. I. and Kien, C. L. Biotinidase deficiency: The enzymatic defect in late-onset multiple carboxylase deficiency. Clin. Chim. Acta 131 (1983a) 273–281
Wolf, B, Grier, R. E., Allen, R. J., Goodman, S. I., Kien, C. L., Parker, W. D., Howell, D. M. and Hurst, D. L. Phenotype variation in biotinidase deficiency. J. Pediatr. 103 (1983b) 233–241
Wolf, B., Hsia, Y. E. and Rosenberg, L. E. Biochemical differences between mutant propionyl CoA carboxylases from two complementation groups. Am. J. Hum. Genet. 30 (1977) 455–464
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© 1985 SSIEM and MTP Press Limited
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Weiner, D.L., Grier, R.E., Wolf, B. (1985). A Bioassay for Determining Biotinidase Activity and for Discriminating Biocytin from Biotin using Holocarboxylase Synthetase-deficient Cultured Fibroblasts. In: Addison, G.M., Bartlett, K., Harkness, R.A., Pollitt, R.J. (eds) Inherited Disorders of Vitamins and Cofactors. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-8019-1_22
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DOI: https://doi.org/10.1007/978-94-011-8019-1_22
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-011-8021-4
Online ISBN: 978-94-011-8019-1
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