A fluorometric assay for biotinidase

Ebrahim, H.; Dakshinamurti, K.

doi:10.1016/0003-2697(86)90527-0

Cited by 39 publications

(13 citation statements)

References 12 publications

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“…A fluorometric assay for the determination of biotinidase activity was carried out, according to Ebrahim and Dekisnamur [14]. Human serum was dialyzed against 50 mM phosphate buffer, pH 7.0 and stored at -20°C prior to use.…”

Section: Methodsmentioning

confidence: 99%

The Effect of Isotretinoin on Biotinidase Activity

Schulpis

Georgala

Papakonstantinou

et al. 1999

Skin Pharmacol Physiol

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Background: Among the reaction and effects of isotretinoin, mucocutaneous reactions, xerosis and erythema of the skin as well as elevation of liver enzymes and lipids except high density lipoprotein have been reported. Objective: Since biotinidase is mainly produced in the liver and partial biotinidase deficiency causes dermatological manifestations, seborrheic dermatitis, alopecia etc., isotretinoin side effects in relation to biotinidase activity were studied. Methods: Forty-two (n = 42) patients with severe cystic acne had liver function tests, lipid estimations, serum biotin as well as biotinidase activity evaluations before (value 1) and on the 30th day (value 2) of treatment with isotretinoin monotherapy (Roaccutane 0.5 mg/kg/24 h). The same laboratory tests were evaluated in 50 controls only once. Moreover, the effect of isotretinoin on a known plasma biotinidase activity was evaluated after incubation in vitro with various concentrations of the drug. Results: A statistically significant elevation of liver enzymes and lipids, except high density lipoprotein, was observed at the end of this study. On the contrary, biotinidase activity was found to be significantly decreased as compared to the initial values (value 1 = 4.70 ± 0.89 nmol/min/l, value 2 = 2.50 ± 0.8 nmol/min/l, p < 0.001) and to controls (5.2 ± 0.9 nmol/min/l vs. value 2 = 2.50 ± 0.8 nmol/min/l, p < 0.001). Additionally, biotin levels showed no significant alterations and the in vitro incubation of the enzyme with various concentrations of the drug exhibited no effect on its activity. Conclusion: It is suggested that isotretinoin isomers-metabolites act in the liver, resulting in low biotinidase activity.

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Section: Methodsmentioning

confidence: 99%

The Effect of Isotretinoin on Biotinidase Activity

Schulpis

Georgala

Papakonstantinou

et al. 1999

Skin Pharmacol Physiol

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“…56 Other assays for biotinidase activity in serum and tissues measure the hydrolysis of biocytin or other biotinyl derivatives. 57,58 Individuals with profound biotinidase deficiency have lower than 10% mean normal serum enzyme activity. Individuals with partial biotinidase deficiency have 10-30% of mean normal serum biotinidase activity.…”

Section: Determination Of Biotinidase Activity In Serum/plasmamentioning

confidence: 99%

Biotinidase deficiency: “if you have to have an inherited metabolic disease, this is the one to have”

Wolf

2012

Genetics in Medicine

159

153

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“…The enzyme was completely or nearly completely inactive toward ε-N-acetyl-L-lysine, ε-N-benzoyl-L-lysine, and ε-N-biotinyl-L--lysine (biocytin) 27) and thus specific for Lipoyl-N-ε-lysine 32) . Therefore, lipoyl-N-ε-lysine is accepted as a reliable substrate for lipoamidase activity assay.…”

Section: Lipoamidase Assaymentioning

confidence: 99%

“…For example, liberated lysine was determined after the reaction with 1, 2-diacetylbenzene but the method requires removal of endogenous lysine from the sample 32) . Other methods reported for the colorimetric determination of thiols and disulfides are not suitable for the detection of small amounts of sulfhydryl compounds like DHLA originated from LA in biological samples [33][34] .…”

Section: Fig 1 Working Of Hypothesis Of the Metabolic Fate Of Externmentioning

confidence: 99%

Activity assay of Lipoamidase, an expected modulator of metabolic fate of externally administered lipoic acid

Wang

Motafakkerazad

Matsugo

et al. 2011

Inflammation and Regeneration

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α-Lipoic acid (LA) is a cofactor functioning in four multienzymes: pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched-chain α-keto acid dehydrogenase, and the glycine cleavage enzyme systems. In each enzyme, LA is covalently bound to the ε-amino group of lysine residues. LA has been used as a medicine for treating diabetic condition in Europe and is also currently a popular supplement resource, and thus the metabolic fate after orally intake of LA attracts much attention whether externally administered LA is incorporated into protein bound form because large fraction of administered dose is not fully explained yet. Lipoamidase is the enzyme catalyzing formation and breakage of amide bond between LA and lysine ε-amino groups in the protein and thus is expected to play critical role in LA metabolism and function. In order to know how the enzyme lipoamidase is involved in the fate of LA in the body, a simple assay method is requested for determining lipoamidase activity in tissues. The method using simple HPLC detection of newly synthesized fluorescent substrate, dansyl-α-lipoyllysine, is discussed together with other previously reported methods. Rec.2/26

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A fluorometric assay for biotinidase

Cited by 39 publications

References 12 publications

The Effect of Isotretinoin on Biotinidase Activity

The Effect of Isotretinoin on Biotinidase Activity

Biotinidase deficiency: “if you have to have an inherited metabolic disease, this is the one to have”

Activity assay of Lipoamidase, an expected modulator of metabolic fate of externally administered lipoic acid

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