An enzyme which catalyzes the release of BIOTIN from biocytin. In human, defects in the enzyme are the cause of the organic acidemia MULTIPLE CARBOXYLASE DEFICIENCY or BIOTINIDASE DEFICIENCY.
The late onset form of MULTIPLE CARBOXYLASE DEFICIENCY (deficiency of the activities of biotin-dependent enzymes propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and PYRUVATE CARBOXYLASE) due to a defect or deficiency in biotinidase which is essential for recycling BIOTIN.
Amidohydrolases are enzymes that catalyze the hydrolysis of amides and related compounds, playing a crucial role in various biological processes including the breakdown and synthesis of bioactive molecules.
A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.
A deficiency in the activities of biotin-dependent enzymes (propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and PYRUVATE CARBOXYLASE) due to one of two defects in BIOTIN metabolism. The neonatal form is due to HOLOCARBOXYLASE SYNTHETASE DEFICIENCY. The late-onset form is due to BIOTINIDASE DEFICIENCY.
A group of disorders characterized by ectodermal-based malformations and neoplastic growths in the skin, nervous system, and other organs.
The neonatal form of MULTIPLE CARBOXYLASE DEFICIENCY that is caused by a defect or deficiency in holocarboxylase synthetase. HLCS is the enzyme that covalently links biotin to the biotin dependent carboxylases (propionyl-CoA-carboxylase, pyruvate carboxylase, and beta-methylcrotonyl-CoA carboxylase).
Incorporation of biotinyl groups into molecules.
An organic mercurial used as a sulfhydryl reagent.

Human biotinidase isn't just for recycling biotin. (1/38)

For years, the major role of biotin has been as the coenzyme for four carboxylases in humans. Although there has been evidence that biotin might have other functions, none has been firmly established. The discovery that human serum biotinidase has biotinyl-transferase activity, in addition to biotinidase hydrolase activity, presents new possibilities for the role of biotinidase in biotin metabolism. Specific transfer of biotin to histones by biotinidase provides a possible explanation for why biotin is found in the nucleus and the nature of its role in the regulation of protein transcription. Future studies will help to determine the functions of biotinidase in biotin metabolism and in disease states.  (+info)

Regulation of leukocyte adherence and migration by glycosylphosphatidyl-inositol-anchored proteins. (2/38)

Leukocyte extravasation is essential for subsequent inflammation and the immune response. Extravasation can be divided into at least three steps; rolling, firm adhesion, and transendothelial migration. Although the mechanisms involved in the first two steps have been fairly well documented, the last step is complex and largely remains to be clarified. This review focuses on the possible role of GPI-anchored proteins on leukocytes in the regulation of their transendothelial migration. In addition to regulation by urokinase and its receptor, which has been regarded as the main modulator, we draw attention to a novel GPI-anchored protein (GPI-80) on human phagocytes that may be involved in regulating leukocyte adhesion and migration. The high degree of homology of GPI-80 with vanin-1, which is expressed on vascular tissues and is involved in prethymic cell homing into the thymus, raises the possibility that there is a family of molecules, including GPI-80 and vanin-1, that may be involved in leukocyte transendothelial migration. The possible role of soluble GPI-anchored proteins in this process is also discussed.  (+info)

Is pantetheinase the actual identity of mouse and human vanin-1 proteins? (3/38)

Pantetheinase is an amidohydrolase involved in the dissimilative pathway of CoA, allowing the turnover of the pantothenate moiety. We have determined the N-terminal sequence as well as the sequences of a number of tryptic and chymotryptic peptides of the protein isolated from pig kidney. These sequence stretches were used as probes to search in the SwissProt database and significant similarities were found with a GPI-anchored protein (mouse vanin-1, with a suggested role in lymphocyte migration), with two putative proteins encoded by human cDNAs (VNN1 and VNN2) and with human biotinidase. On the basis of sequence similarity, we propose that vanin-1 and VNN1 should be identified as pantetheinase.  (+info)

Fine mapping of the human biotinidase gene and haplotype analysis of five common mutations. (4/38)

Biotinidase deficiency is an autosomal recessive defect in the recycling of biotin that can lead to a variety of neurologic and cutaneous symptoms. The disease can be prevented or effectively treated with exogenous biotin. The biotinidase locus (BTD) has been maped to 3p25 by in situ hybridization. The gene has been cloned, the coding region sequenced, the genomic organization determined, and a spectrum of mutations has been characterized in more than 90 individuals with profound or partial biotinidase deficiency. We have conducted haplotype analysis of 10 consanguineous and 39 nonconsanguineous probands from the United States and 8 consanguineous probands from Turkey to localize BTD with respect to polymorphic markers on 3p and to investigate the origins of five common mutations. The inbred probands were homozygous for overlapping regions of 3p ranging in size from 1.1 to 80 cM which were flanked most narrowly by D3S1259 and D3S1293. Radiation hybrids and haplotype analysis of markers within this region suggest that BTD is located within a 0.1-cM region flanked by D3S3510 and D3S1286. The radiation hybrid data suggest that the BTD gene is oriented 5' to 3' between the centromere and the 3p telomere. Association studies indicate that the gene is closer to a third locus D3S3613 than D3S3510, two markers which cannot be resolved by existing linkage data. The BTD locus and D3S3613 must therefore lie between D3S3510 and D3S1286. Comparison of haplotypes reveals evidence for possible founder effects for four of the five common mutations.  (+info)

Molecular characterisation of 34 patients with biotinidase deficiency ascertained by newborn screening and family investigation. (5/38)

This study characterises the spectrum of biotinidase mutations in 21 patients (17 families) with profound biotinidase deficiency (BD) and 13 unrelated patients with partial BD using a denaturing gradient gel electrophoretic mutation screening and selective sequencing approach. In 29 from 30 unrelated families we found biallelic mutations including four common mutations, D444H (frequency 23.3%), G98:d7i3(20.0%), Q456H(20.0%), T532M (15.0%) and nine rare mutations (V62M, R157H, A171T+D444H, C423W, D543H, L279W, N172S, V109G, 12236G-A) with frequencies less than 5.0%. Only three profound BD patients with G98:d7i3/G98:d7i3 and Q456H/Q456H genotypes and residual biotinidase activities of 0.0%, and 0.9% of normal activity developed clinical symptoms before biotin supplementation at 8 weeks of age. All other patients remained asymptomatic within the first months of life or even longer without treatment. Two patients homozygous for the frameshift mutation G98:d7i3 had no measurable residual enzyme activity. Twelve patients with partial BD had the D444H mutation in at least one allele. We conclude that, based on mutation analysis and biochemical examinations of the enzyme, it is currently not clearly predictable whether an untreated patient will develop symptoms or not, although it seems that patients with activities lower than 1% are at a high risk for developing symptoms of the disease early in life.  (+info)

Biotinylation of histones in human cells. Effects of cell proliferation. (6/38)

An enzymatic mechanism has been proposed by which biotinidase may catalyze biotinylation of histones. Here, human cells were found to covalently bind biotin to histones H1, H2A, H2B, H3, and H4. Cells respond to proliferation with increased biotinylation of histones; biotinylation increases early in the cell cycle and remains increased during the cycle. Notwithstanding the catalytic role of biotinidase in biotinylation of histones, mRNA encoding biotinidase and biotinidase activity did not parallel the increased biotinylation of histones in proliferating cells. Biotinylation of histones might be regulated by enzymes other than biotinidase or by the rate of histone debiotinylation.  (+info)

Biotin dependency due to a defect in biotin transport. (7/38)

We describe a 3-year-old boy with biotin dependency not caused by biotinidase, holocarboxylase synthetase, or nutritional biotin deficiency. We sought to define the mechanism of his biotin dependency. The child became acutely encephalopathic at age 18 months. Urinary organic acids indicated deficiency of several biotin-dependent carboxylases. Symptoms improved rapidly following biotin supplementation. Serum biotinidase activity and Biotinidase gene sequence were normal. Activities of biotin-dependent carboxylases in PBMCs and cultured skin fibroblasts were normal, excluding biotin holocarboxylase synthetase deficiency. Despite extracellular biotin sufficiency, biotin withdrawal caused recurrent abnormal organic aciduria, indicating intracellular biotin deficiency. Biotin uptake rates into fresh PBMCs from the child and into his PBMCs transformed with Epstein Barr virus were about 10% of normal fresh and transformed control cells, respectively. For fresh and transformed PBMCs from his parents, biotin uptake rates were consistent with heterozygosity for an autosomal recessive genetic defect. Increased biotin breakdown was ruled out, as were artifacts of biotin supplementation and generalized defects in membrane permeability for biotin. These results provide evidence for a novel genetic defect in biotin transport. This child is the first known with this defect, which should now be included in the identified causes of biotin dependency.  (+info)

PCR designer for restriction analysis of various types of sequence mutation. (8/38)

Restriction analysis is widely used to detect gene mutations such as insertions, deletions and single nucleotide polymorphisms (SNPs). Although such mutation sites sometimes present some natural restriction sites to differentiate the wild-type and mutant sequences, mismatches are often needed in order to create artificial restriction fragment length polymorphisms (RFLPs). In this report, a computer program is described that screens for suitable restriction enzymes, introducing mismatches where appropriate and when necessary, designs primers using the information of the selected restriction enzymes, their recognition sequence and locations as well as the information about the mismatches if any. The program, supported by a WWW web interface, is intended to be used online.  (+info)

Biotinidase is an enzyme that is responsible for the release of biotin, a vital nutrient, from proteins in the body. Biotin is essential for various metabolic processes, including the synthesis of fatty acids and glucose. Biotinidase deficiency can lead to serious health problems, such as seizures, developmental delays, and hearing and vision loss. Therefore, biotinidase levels are often measured in newborn screening tests to identify babies who may be at risk for this rare but treatable condition.

Biotinidase deficiency is a genetic disorder that affects the body's ability to recycle and reuse biotin, a type of B vitamin. Biotinidase is an enzyme that helps release biotin from proteins in the food we eat and recycle it for use by the body.

In people with biotinidase deficiency, the biotinidase enzyme is either partially or completely missing, leading to a decrease in available biotin. This can result in a variety of symptoms, including seizures, developmental delays, hearing and vision loss, skin rashes, hair loss, and muscle weakness.

There are two main types of biotinidase deficiency: partial deficiency and profound deficiency. Partial deficiency means that some biotinidase activity is present, but not enough to prevent symptoms. Profound deficiency means that there is little or no biotinidase activity, resulting in more severe symptoms.

Biotinidase deficiency can be diagnosed through a blood test that measures the level of biotinidase enzyme activity. Treatment typically involves taking biotin supplements to replace the missing biotin and prevent symptoms from developing or worsening. With early diagnosis and treatment, people with biotinidase deficiency can often lead normal lives.

Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).

The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.

Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.

Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.

Biotin is a water-soluble vitamin, also known as Vitamin B7 or Vitamin H. It is a cofactor for several enzymes involved in metabolism, particularly in the synthesis and breakdown of fatty acids, amino acids, and carbohydrates. Biotin plays a crucial role in maintaining healthy skin, hair, nails, nerves, and liver function. It is found in various foods such as nuts, seeds, whole grains, milk, and vegetables. Biotin deficiency is rare but can occur in people with malnutrition, alcoholism, pregnancy, or certain genetic disorders.

Multiple carboxylase deficiency (MCD) is a rare genetic disorder that affects the body's ability to metabolize certain amino acids, particularly those that contain sulfur. It is caused by mutations in the genes responsible for producing enzymes involved in the biotin-dependent carboxylation reactions, which are critical for various metabolic processes in the body.

There are two major types of MCD:

1. Profound multiple carboxylase deficiency (also known as Type II biotinidase deficiency): This form is more severe and is caused by a defect in the holocarboxylase synthetase enzyme, which is responsible for attaching biotin to several carboxylases.
2. Biotin-responsive multiple carboxylase deficiency (also known as Type I biotinidase deficiency): This form is milder and is caused by a defect in the biotinidase enzyme, which recycles biotin in the body. However, it can be treated with biotin supplementation.

Symptoms of MCD may include:

* Developmental delay
* Seizures
* Hypotonia (low muscle tone)
* Ataxia (lack of coordination)
* Rash
* Hair loss
* Acidosis (high levels of acid in the body)
* Coma and even death, if left untreated

Early diagnosis and treatment with biotin supplementation can significantly improve outcomes for individuals with MCD.

Neurocutaneous syndromes are a group of rare, genetic disorders that primarily affect the nervous system and skin. These conditions are present at birth or develop in early childhood. They are characterized by the growth of benign tumors along nerve pathways (neurocutaneous) and various abnormalities of the skin, eyes, brain, spine, and other organs.

Some common examples of neurocutaneous syndromes include:

1. Neurofibromatosis type 1 (NF1): A condition characterized by multiple café-au-lait spots on the skin, freckling in the axillary and inguinal regions, and neurofibromas (benign tumors of the nerves).
2. Neurofibromatosis type 2 (NF2): A condition that primarily affects the auditory nerves and is characterized by bilateral acoustic neuromas (vestibular schwannomas), which can cause hearing loss, tinnitus, and balance problems.
3. Tuberous sclerosis complex (TSC): A condition characterized by benign tumors in various organs, including the brain, skin, heart, kidneys, and lungs. The skin manifestations include hypomelanotic macules, facial angiofibromas, and shagreen patches.
4. Sturge-Weber syndrome (SWS): A condition characterized by a port-wine birthmark on the face, which involves the trigeminal nerve distribution, and abnormal blood vessels in the brain, leading to seizures, developmental delays, and visual impairment.
5. Von Hippel-Lindau disease (VHL): A condition characterized by the growth of benign tumors in various organs, including the brain, spinal cord, kidneys, pancreas, and adrenal glands. The tumors can become malignant over time.
6. Ataxia-telangiectasia (A-T): A condition characterized by progressive ataxia (loss of coordination), oculocutaneous telangiectasias (dilated blood vessels in the skin and eyes), immune deficiency, and increased risk of cancer.

Early diagnosis and management of neurocutaneous disorders are essential to prevent complications and improve outcomes. Regular follow-up with a multidisciplinary team, including neurologists, dermatologists, ophthalmologists, geneticists, and other specialists, is necessary to monitor disease progression and provide appropriate interventions.

Holocarboxylase Synthetase Deficiency (HCD) is a rare genetic disorder of biotin metabolism, characterized by the body's inability to properly utilize the vitamin biotin. Biotin plays a crucial role in various essential functions, such as the breakdown of fats, proteins, and carbohydrates, as well as the regulation of gene expression.

Holocarboxylase synthetase is an enzyme responsible for attaching biotin to four different carboxylases, which are necessary for these vital processes. In Holocarboxylase Synthetase Deficiency, this enzyme is either partially or completely nonfunctional due to mutations in the HLCS gene.

The symptoms of HCD can vary widely but often include:

1. Feeding difficulties and poor growth in infancy
2. Severe metabolic acidosis
3. Ketoacidosis
4. Delayed development
5. Hypotonia (low muscle tone)
6. Skin rashes
7. Hair loss
8. Neurological symptoms, such as seizures and ataxia (loss of coordination and balance)

If left untreated, Holocarboxylase Synthetase Deficiency can lead to severe complications, including developmental delays, neurological damage, and even death. However, with early diagnosis and proper treatment involving biotin supplementation, many of these symptoms can be managed, and the progression of the disorder can be slowed or stopped.

Biotinyllation is a process of introducing biotin (a vitamin) into a molecule, such as a protein or nucleic acid (DNA or RNA), through chemical reaction. This modification allows the labeled molecule to be easily detected and isolated using streptavidin-biotin interaction, which has one of the strongest non-covalent bonds in nature. Biotinylated molecules are widely used in various research applications such as protein-protein interaction studies, immunohistochemistry, and blotting techniques.

P-Chloromercuribenzoic acid (CMB) is not primarily considered a medical compound, but rather an organic chemical one. However, it has been used in some medical research and diagnostic procedures due to its ability to bind to proteins and enzymes. Here's the chemical definition:

P-Chloromercuribenzoic acid (CMB) is an organomercury compound with the formula C6H4ClHgO2. It is a white crystalline powder, soluble in water, and has a melting point of 208-210 °C. It is used as a reagent to study protein structure and function, as it can react with sulfhydryl groups (-SH) in proteins, forming a covalent bond and inhibiting their activity. This property has been exploited in various research and diagnostic applications. However, due to its toxicity and environmental concerns related to mercury, its use is now limited and regulated.

Biotinidase (EC 3.5.1.12, amidohydrolase biotinidase, BTD), also known as biotinase, is an enzyme that in humans is encoded by ... Biotinidase deficiency is an inherited disorder caused by mutations in the BTD gene. When biotinidase activity is deficient, ... Mutations in the BTD gene cause biotinidase deficiency. Approximately 100 mutations in the BTD gene that lead to biotinidase ... Without biotinidase activity, the vitamin biotin cannot be separated from foods and therefore cannot be used by the body. ...
Biotinidase deficiency is an inherited disorder in which the body is unable to recycle the vitamin biotin. Explore symptoms, ... Profound biotinidase deficiency results when the activity of biotinidase is reduced to less than 10 percent of normal. Partial ... Wolf B. Biotinidase deficiency: if you have to have an inherited metabolic disease, this is the one to have. Genet Med. 2012 ... Biotinidase removes biotin that is bound to proteins in food, leaving the vitamin in its free (unbound) state. Free biotin is ...
Biotinidase (BTD), a ubiquitous mammalian cell enzyme, is present in high levels in the serum, liver, and kidneys. Its primary ... Profound biotinidase deficiency has an incidence of about 1 per 137,400 population; partial biotinidase deficiency affects ... encoded search term (Biotinidase Deficiency) and Biotinidase Deficiency What to Read Next on Medscape ... This inborn error of metabolism can result from either partial or complete absence of biotinidase. Biotinidase deficiency has a ...
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Preferred test for the diagnosis of biotinidase deficiency Follow-up testing for certain organic acidurias ... Biotinidase deficiency is an autosomal recessive disorder caused by variants in the biotinidase gene (BTD). Age of onset and ... When biotinidase enzyme activity is deficient, sequencing of the entire BTD gene (BTDZ / Biotinidase Deficiency, BTD Full Gene ... Profound biotinidase deficiency occurs in approximately 1 in 137,000 live births and partial biotinidase deficiency occurs in ...
Localization of biotinidase in the brain: implications for its role in hearing loss in biotinidase deficiency. Hear Res 2002; ... Biotinidase deficiency. Biotinidase deficiency is secondary to absence of the water-soluble B-complex vitamin biotin. Biotin ... If biotinidase deficiency is not recognized and corrected by daily addition of biotin to the diet, affected persons develop ... Wolf B, Spencer R, Gleason T . Hearing loss is a common feature of symptomatic children with profound biotinidase deficiency. J ...
Biotinidase in blood probably originates from the liver. Biotinidase in serum is sialylated, but in rat liver from which blood ... Biotinidase in blood probably originates from the liver. Biotinidase in serum is sialylated, but in rat liver from which blood ... Biotinidase in blood probably originates from the liver. Biotinidase in serum is sialylated, but in rat liver from which blood ... Biotinidase in blood probably originates from the liver. Biotinidase in serum is sialylated, but in rat liver from which blood ...
Biotinidase. Category. Biochemistry Test background. Biotinidase deficiency is an autosomal recessive metabolic disorder of ... Symptoms of untreated biotinidase deficiency may appear at any time from 1 week to 10 years of age. The most common early ...
5. Biotinidase deficiency. This hereditary disorder is very rare. It prevents your body from reusing biotin. Typically, the ... People with biotinidase deficiency. This rare hereditary disorder prevents the body from reusing biotin. People with the ... Biotinidase deficiency. (2017).. https://ghr.nlm.nih.gov/condition/biotinidase-deficiency. *. Dietary reference intakes (DRIs ...
What if it was not RA, but adult Biotinidase Deficiency instead?. There are too many things I need and want to say to put into ... We also learned that there is a name for this disease, it is Biotinidase Deficiency. They say 1:60,000 babies are born with it ... Research has told her that Biotinidase Deficiency could be the cause of her food allergies; she cannot wait to try an avocado ...
Individuals with partial biotinidase deficiency may have hypotonia, skin rash, and hair loss, particularly during times of ... Older children and adolescents with profound biotinidase deficiency often exhibit motor limb weakness, spastic paresis, and ... young children with profound biotinidase deficiency usually exhibit neurologic abnormalities including seizures, hypotonia, ... Biotinidase Deficiency. American College of Medical Genetics Algorithm, Biotinidase Deficiency, 2022. American College of ...
... consistent with biotinidase deficiency. Biotinidase activity was recorded as 0.5 nmol/mL/min, confirming the diagnosis. The ... Biotinidase deficiency is a treatable cause of infantile epilepsy and the presentation can be nonspecific. The seizures are ... Biotinidase activity was low at 0.4 nmol/mL/min. Treatment with phenobarbital was instituted at presentation, followed by ... I had a female patient with biotinidase deficiency who presented at 3 years of age with ataxia. Serum lactate was 33 (,20). CSF ...
Biotinidase deficiency: Same-day TAT. Health and Medicine Reference Covering Thousands of Diseases and Prescription Drugs. ... Biotinidase deficiency. Biotinidase deficiency is an inherited disorder in which the body is not able to process the vitamin ... Mutations in the BTD gene cause biotinidase deficiency. Biotinidase is the enzyme that is made by the BTD gene. Many mutations ... Biotinidase deficiency. Bipolar disorder. Birt-Hogg-Dube syndrome. Blastoma. Blastomycosis. Blepharitis. Blepharospasm. Bloom ...
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Biotinidase deficiency. Sources: Raghuveer TS, Garg U, Graf WD. Inborn errors of metabolism in infancy and early childhood: an ...
Biotinidase deficiency D81.818 Other biotin-dependent carboxylase deficiency D81.89 Other combined immunodeficiencies ...
Deficient biotinidase activity in late-onset multiple carboxylase deficiency. N Engl J Med. 1983 Jan 20. 308(3):161. [QxMD ...
Biotinidase Deficiency. These keywords were added by machine and not by the authors. This process is experimental and the ...
N-D-biotinyl-7-amino-4-methylcoumarin as a novel fluoreigenic substrate for the determination of biotinidase activity ...
Biotinidase Deficiency 1:60,000 Severe Combined Immunodeficiency (SCID) 1:100,000 Mucopolysaccharidosis Type I (MPS-I) 1: ...
Biotinidase deficiency: MedlinePlus Genetics (National Library of Medicine) * Childhood myocerebrohepatopathy spectrum: ...
Biotinidase deficiency. Carnitine palmitoyltransferase II deficiency. Carnitine uptake defect. Citrullinemia, type I. Cobalamin ...
Biotinidase deficiency. An enzyme is missing resulting in a deficiency in biotin. This deficiency can lead to seizures, hearing ...
Biotinidase Deficiency (BIOT). To detect conditions where the infant is unable to recycle biotin (vitamin) leading to a ... biotinidase (BIOT), cystic fibrosis (CF), severe combined immunodeficiency (SCID) and inborn errors of metabolism (IEM) by MS/ ...
Biotinidase deficiency. *Galactosemia. *Glycogen storage disorders. *Homocystinuria. *Maple syrup urine disease (MSUD) ...
Administration of large doses of biotin is dramatically successful in cases of biotinidase deficiency.9 For the remaining ...
BIOT) Biotinidase deficiency*. *(CF) Cystic Fibrosis*. *(SCID) Severe Combined Immunodeficiency*. *(GALT) Classic Galactosemia* ...
have a biotinidase deficiency, meaning that the body is unable to release biotin from dietary protein ...
Biotin label with a biotinidase-resistant linkage. *Fixable primary amine. *Used for visualizing neural architecture and for ...

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