Re: Can biotin cause yeast die-off?

[Guest guest]

Hi ,

I believe biotin can cause yeast die-off from what I've seen on the

other boards. we just started using it also.

>

> Hello everyone,

>

> I know that Biotin works with the body to produce good bacteria and

> keep yaest in check. Right? Anyway, can it cause yeast die-off?

>

> Just Curious,

>

>

[Guest guest]

,

You said:

>I believe biotin can cause yeast die-off from what I've seen on the

>other boards. we just started using it also.

That could happen, but I'd like to explain WHY it might happen and some

other things it would be good to know about biotin.

Biotin is a cofactor for a whole class of enzymes called carboxylases that

are used by us and our flora.

Biotin works as a swinging arm inside those molecules which allows the

enzymes to do their job. Carboxylases (and also some biotin-dependent

decarboxylases, especially in bacteria) have many functions, but the best

way to understand those functions is to look at the list of things that

might happen to you if you have biotin deficiency or a deficiency of the

enzyme that recycles biotin or another reason for these enzymes to be

impaired..

One influence we've just learned about in recent years is oxalate, a very

reactive molecule found to be high in some plant foods that if it gets

absorbed through a leaky gut, and finds a carboxylase enzyme, it will

replace another cofactor in the enzyme complex that usually hooks to biotin

and makes the enzyme work. Unfortunately, the oxalate keeps that swinging

arm from accomplishing the job of the enzyme.

Because there are so many ways that biotin's job can be hindered,it is

sometimes appropriate to take biotin in doses that are far higher than the

RDA and it is not unusual for an effective dose to get as high as 10

mgs. Having greater than normal amounts of biotin around will help most of

these problems, but it is also a very good idea to spend some time figuring

out what caused the biotin problem in the first place and see if you can

correct that. Ideas about that are below!

Here is a list of things that go wrong in biotin deficiency and you will

notice it includes problems with yeast infections which finally gets to

your question! The problems with yeast are believed to derive from a lack

of proper immune defense agains candida. What might change in regards to

yeast when you've taken biotin is that the immune system may be suddenly

enabled to start to recognize the problem in overgrowth and start to kill

the candida. That may explain the die-off that did not come from using any

anti-anything medicine, but instead from enabling immune defense. You have

to wonder why that immune defense is so often not up to the task of keeping

yeast within bounds in autism and some other conditions.

Anyway, this is a list of other biotin-deficiency related symptoms:

hypotonia

ataxia

hair loss (alopecia)

seizures

encephalopathy

neurodevelopmental delay

motor limb weakness

loss of visual acuity

hearing loss

chronic candidiasis

Immunological deficiencies especially cellular immunity abnormalities

Breathing abnormalities including apnea, hyperventilation, and laryngeal

stridor.

swallowing difficulties

jaundice

secretory diarrhea

eczematous and other skin rashes (dermatitis)

metabolic acidosis

ketolacticacidosis

hemianopia

optic atrophy

Leigh syndrome

spastic paraparesis

The lab test for biotin deficiency finds the following elevated in a

urinary organic acid test, but you won't see all these reported on typical

OATs we get in the autism community:

3-Methylcrotonylglycine

3-Hydroxyisovaleric acid

3-Hydroxypropionic acid

Methylcitric acid

The carboxylase enzymes also need CoA, which is a product of pantothenic

acid and cysteine and ADP. That means if there is not enough

intracellular cysteine around to make enough CoA, biotin-dependent enzymes

may not work well and you might also see some problems with energy.

Apparently, one of the mechanisms that might break down with low

intracellular biotin might be the handling of the ammonia that is produced

when glutamine is converted into glutamate: an important step for the

making of inhibitory GABA and for making glutathione.

I think that the people who are most likely to respond to biotin are those

who have used biotin depleters. This can include anticonvulsants such as

phenytoin, primidone, carbamezepine, and phenobarbital which may incease

urinary excretion of biotin. Valproic acid or depakote can cause

biotinidase deficiency, which is a problem in recycling biotin. I have yet

to meet a child with autism on depakote that progressed with biomedical

interventions as much as other children, and I wonder if this might be why.

I would like to also mentione alpha lipoic acid because it competes with

biotin for transport, as discussed in an article below. That means the

biotin you got from your diet or from your flora may not have competed well

for absorption in the gut or for reabsorption in the kidneys, and that may

mean that your would-have-been adequate biotin may have ended up in the

toilet. For children who were biotin depleted because of use of

antibiotics which killed their biotin-making flora or because of being on

depakote, this loss of reabsorption may have more serious consequences.

There are tests to measure lack of activity of certain biotin dependent

carboxylases, mainly using the organic acid profile. It seems

3-hydroxyisovaleric acid is the first one that moves during deficiency, but

the others come " online " if you get really deficient or under stress. Here

below I've put a listing of the different carboxylases, and which markers

are associated with deficient activity of each one.

These enzymes may have a lot of organ specificity, because we know that

some people with biotin-responsive conditions in the brain have not had

these markers in the urine so don't assume if you lack these markers that

biotin won't do you some good.

For those who want to know more, there is a mini-section on biotin that I

wrote a number of years ago that was included in the very back of the DAN!

manual that was written and edited by Jon Pangborn and Sid Baker.

I hope this helps.

Enzyme

Acetyl-CoA Carboxylase (cytosolic active ACC1 and mitochondrially active ACC2)

*most enhanced by supplement of biotin

sensitive to insulin

Reaction

ATP+ acetyl-CoA+ HCO(3)(-) <=>ADP+ phosphate + malonyl-CoA

Organic acid deficiency marker:

elevated hexanoic acid

including 2-ethyl-3-keto-hexanoic

2-ethyl-3-hydroxy-hexanoic acid

2-ethyl-hexanedioic acid

---------------------------------------------------

Enzyme

Pyruvate Carboxylase

Reaction

ATP+ pyruvate+ HCO(3)(-) <=>ADP+ phosphate + oxaloacetate

Deficiency markers:

lactic acidemia

hyperammonemia, and citrullinemia

hyperlysinemia

decreased beta hydroxybutyrate/acetoacetate ratio

------------------------------------------------------

Enzyme

propionyl-CoA carboxylase

Reaction catalyzed

(S)-2-methyl-3-oxopropanoyl-CoA <=> propanoyl-CoA + CO(2)

Deficiency marker in organic acid profile:

elevated 3-hydroxypropionic acid

elevated methylcitrate

--------------------------------------------------------

Enzyme

beta-methylcrotonyl-CoA carboxylase

Reaction

ATP+ 3-methylcrotonyl-CoA + HCO(3)(-)

<=>ADP+ phosphate + 3-methylglutaconyl-CoA

Organic acid deficiency marker:

elevated 3-Methylcrotonylglycine

elevated 3-Hydroxyisovaleric acid

also: secondary carnitine deficiency

--------------------------------------------------------

J Gastroenterol 1995 Jun;30(3):351-5 Related Articles, Books, LinkOut

Effect of biotin on ammonia intoxication in rats and mice.

Nagamine T, Saito S, Kaneko M, Sekiguchi T, Sugimoto H, Takehara K,

Takagi H.

First Department of Internal Medicine, Gunma University School of

Medicine, Maebashi, Japan.

The effects of biotin on ammonia concentration in blood and brain were

evaluated in hyperammonemic rats and mice. Rats were injected with 5

mmol/kg BW of ammonium acetate, and mice were injected with 10 mmol/kg BW.

Increases in blood ammonia levels in rats 15-30 min after ammonia loading

were prevented by treatment with 0.2 ml/100 g BW of biotin or 0.04 ml/100 g

BW of arginine-glutamate with statistical significance. Blood ammonia

levels after ammonia loading were lower, although not significantly, in the

arginine glutamate-treated rats than in the biotin-treated animals. In mice

also, increases in blood and brain ammonia levels after ammonia loading

were prevented by the administration of biotin. The decrease in brain

glutamate and aspartate after ammonia loading was lower and the brain

glutamine level was higher in biotin-treated mice than in the controls.

These findings indicate the protective effect of biotin against ammonia

intoxication.

PMID: 7647902 [PubMed - indexed for MEDLINE]

J Nutr 1997 Sep;127(9):1776-81 Related Articles, Books, LinkOut

[Click here to read]

Lipoic acid reduces the activities of biotin-dependent carboxylases in

rat liver.

Zempleni J, Trusty TA, Mock DM.

Department of Pediatrics, University of Arkansas for Medical Sciences

and the Arkansas Children's Hospital Research Institute, Little Rock, AR

72202, USA.

In the past, lipoic acid has been administered to patients and test

animals as therapy for diabetic neuropathy and various intoxications.

Lipoic acid and the vitamin biotin have structural similarities. We sought

to determine whether the chronic administration of lipoic acid affects the

activities of biotin-dependent carboxylases. For 28 d, rats received daily

intraperitoneal injections of one of the following: 1) a small dose of

lipoic acid [4.3 micromol/( kg.d)]; 2) a large dose of lipoic acid [15.6

micromol/(kg.d)]; or 3) a large dose of lipoic acid plus biotin [15.6 and

2.0 micromol/(kg.d), respectively]. Another group received n-hexanoic acid

[14.5 micromol/(kg.d)], which has structural similarities to lipoic acid

and biotin and thus served as a control for the specificity of lipoic acid.

A fifth group received phosphatidylcholine in saline injections and served

as the vehicle control. The rat livers were assayed for the activities of

acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase,

and beta-methylcrotonyl-CoA carboxylase. Urine was analyzed for lipoic

acid; serum was analyzed for indicators of liver damage and metabolic

aberrations. The mean activities of pyruvate carboxylase and

beta-methylcrotonyl-CoA carboxylase were 28-36% lower in the lipoic

acid-treated rats compared with vehicle controls (P < 0.05). Rats treated

with lipoic acid plus biotin had normal carboxylase activities. Carboxylase

activities in livers of n-hexanoic acid-treated rats were normal despite

some evidence of liver injury. Propionyl-CoA carboxylase and acetyl-CoA

carboxylase were not significantly affected by administration of lipoic

acid. This study provides evidence consistent with the hypothesis that

chronic administration of lipoic acid lowers the activities of pyruvate

carboxylase and beta-methylcrotonyl-CoA carboxylase in vivo by competing

with biotin.

PMID: 9278559 [PubMed - indexed for MEDLINE]

At 01:04 PM 1/19/2008, you wrote:

>Hi ,

>

>I believe biotin can cause yeast die-off from what I've seen on the

>other boards. we just started using it also.

>

>

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Checked by AVG Free Edition.

Version: 7.5.503 / Virus Database: 269.17.8/1196 - Release Date: 12/25/2007

12:18 PM

[Guest guest]

So ,

Are you saying if you give lipoic acid you should also be giving

Biotin or are you saying don't give lipoic acid?

Alice

>

> >Hi ,

> >

> >I believe biotin can cause yeast die-off from what I've seen on

the

> >other boards. we just started using it also.

> >

> >

>

>

> --

> Internal Virus Database is out-of-date.

> Checked by AVG Free Edition.

> Version: 7.5.503 / Virus Database: 269.17.8/1196 - Release Date:

12/25/2007 12:18 PM

>

[Guest guest]

,

Thank you for all of your Oxalate research my child is exactly what you write about...He has Oxalate issue's and it took me about a year to figure out why the dilation of the eye's....Bingo Oxalate's! homemade goat's yogurt has helped us deal with our Oxalate issue...We give it at the same time as the Oxalate meal and it work's because there is no dilation with the Strawberries etc. Thank you for all your hard work! My child also has severe glutamate issue's....ex: when he get's a hold of any corn ingredient he become's unable to understand anything that he just understood hours prior...Do you have any suggestion's to help out with glutamate issue's? and will chelation get rid of these issue's or will he allow's have these issue's?

Thanks,

Dana C. Sturdivant

-------------- Original message from Owens : --------------

,You said:>I believe biotin can cause yeast die-off from what I've seen on the>other boards. we just started using it also.That could happen, but I'd like to explain WHY it might happen and some other things it would be good to know about biotin.Biotin is a cofactor for a whole class of enzymes called carboxylases that are used by us and our flora.Biotin works as a swinging arm inside those molecules which allows the enzymes to do their job. Carboxylases (and also some biotin-dependent decarboxylases, especially in bacteria) have many functions, but the best way to understand those functions is to look at the list of things that might happen to you if you have biotin deficiency or a deficiency of the enzyme that recycles biotin or another reason for these enzymes to be impaired..One influence we've just learned about in recent years is oxalate, a very reactive molecule found to be high in some plant foods that if it gets absorbed through a leaky gut, and finds a carboxylase enzyme, it will replace another cofactor in the enzyme complex that usually hooks to biotin and makes the enzyme work. Unfortunately, the oxalate keeps that swinging arm from accomplishing the job of the enzyme.Because there are so many ways that biotin's job can be hindered,it is sometimes appropriate to take biotin in doses that are far higher than the RDA and it is not unusual for an effective dose to get as high as 10 mgs. Having greater than normal amounts of biotin around will help most of these problems, but it is also a very good idea to spend some time figuring out what caused the biotin problem in the first place and see if you can correct that. Ideas about that are below!Here is a list of things that go wrong in biotin deficiency and you will notice it includes problems with yeast infections which finally gets to y

our question! The problems with yeast are believed to derive from a lack of proper immune defense agains candida. What might change in regards to yeast when you've taken biotin is that the immune system may be suddenly enabled to start to recognize the problem in overgrowth and start to kill the candida. That may explain the die-off that did not come from using any anti-anything medicine, but instead from enabling immune defense. You have to wonder why that immune defense is so often not up to the task of keeping yeast within bounds in autism and some other conditions.Anyway, this is a list of other biotin-deficiency related symptoms:hypotoniaataxiahair loss (alopecia)seizuresencephalopathyneurodevelopmental delaymotor limb weaknessloss of visual acuityhearing losschronic candidiasisImmunological deficiencies especially cellular immunity abnormalitiesBreathing abnormalities including apnea, hype

rventilation, and laryngeal stridor.swallowing difficultiesjaundicesecretory diarrheaeczematous and other skin rashes (dermatitis)metabolic acidosisketolacticacidosishemianopiaoptic atrophyLeigh syndromespastic paraparesisThe lab test for biotin deficiency finds the following elevated in a urinary organic acid test, but you won't see all these reported on typical OATs we get in the autism community:3-Methylcrotonylglycine3-Hydroxyisovaleric acid3-Hydroxypropionic acidMethylcitric acidThe carboxylase enzymes also need CoA, which is a product of pantothenic acid and cysteine and ADP. That means if there is not enough intracellular cysteine around to make enough CoA, biotin-dependent enzymes may not work well and you might also see some problems with energy.Apparently, one of the mechanisms that might break down with low intracellular biotin might be the handling of the

ammonia that is produced when glutamine is converted into glutamate: an important step for the making of inhibitory GABA and for making glutathione.I think that the people who are most likely to respond to biotin are those who have used biotin depleters. This can include anticonvulsants such as phenytoin, primidone, carbamezepine, and phenobarbital which may incease urinary excretion of biotin. Valproic acid or depakote can cause biotinidase deficiency, which is a problem in recycling biotin. I have yet to meet a child with autism on depakote that progressed with biomedical interventions as much as other children, and I wonder if this might be why.I would like to also mentione alpha lipoic acid because it competes with biotin for transport, as discussed in an article below. That means the biotin you got from your diet or from your flora may not have competed well for absorption in the gut or for reabsorption in the kidney

s, and that may mean that your would-have-been adequate biotin may have ended up in the toilet. For children who were biotin depleted because of use of antibiotics which killed their biotin-making flora or because of being on depakote, this loss of reabsorption may have more serious consequences.There are tests to measure lack of activity of certain biotin dependent carboxylases, mainly using the organic acid profile. It seems 3-hydroxyisovaleric acid is the first one that moves during deficiency, but the others come "online" if you get really deficient or under stress. Here below I've put a listing of the different carboxylases, and which markers are associated with deficient activity of each one.These enzymes may have a lot of organ specificity, because we know that some people with biotin-responsive conditions in the brain have not had these markers in the urine so don't assume if you lack these markers that biotin won't do you some good.For those who want to know more, there is a mini-section on biotin that I wrote a number of years ago that was included in the very back of the DAN! manual that was written and edited by Jon Pangborn and Sid Baker.I hope this helps.EnzymeAcetyl-CoA Carboxylase (cytosolic active ACC1 and mitochondrially active ACC2)*most enhanced by supplement of biotinsensitive to insulinReactionATP+ acetyl-CoA+ HCO(3)(-) <=>ADP+ phosphate + malonyl-CoAOrganic acid deficiency marker:elevated hexanoic acidincluding 2-ethyl-3-keto-hexanoic2-ethyl-3-hydroxy-hexanoic acid2-ethyl-hexanedioic acid---------------------------------------------------EnzymePyruvate CarboxylaseReactionATP+ pyruvate+ HCO(3)(-) <=>ADP+ phosphate + oxaloacetateDeficiency markers:lactic acidemiahyperammonemia, and citrullinemi

ahyperlysinemiadecreased beta hydroxybutyrate/acetoacetate ratio------------------------------------------------------Enzymepropionyl-CoA carboxylaseReaction catalyzed(S)-2-methyl-3-oxopropanoyl-CoA <=> propanoyl-CoA + CO(2)Deficiency marker in organic acid profile:elevated 3-hydroxypropionic acidelevated methylcitrate--------------------------------------------------------Enzymebeta-methylcrotonyl-CoA carboxylaseReactionATP+ 3-methylcrotonyl-CoA + HCO(3)(-) <=>ADP+ phosphate + 3-methylglutaconyl-CoAOrganic acid deficiency marker:elevated 3-Methylcrotonylglycineelevated 3-Hydroxyisovaleric acidalso: secondary carnitine deficiency--------------------------------------------------------J Gastroenterol 1995 Jun;30(3):351-5 Related Articles, B

ooks, LinkOutEffect of biotin on ammonia intoxication in rats and mice.Nagamine T, Saito S, Kaneko M, Sekiguchi T, Sugimoto H, Takehara K, Takagi H.First Department of Internal Medicine, Gunma University School of Medicine, Maebashi, Japan.The effects of biotin on ammonia concentration in blood and brain were evaluated in hyperammonemic rats and mice. Rats were injected with 5 mmol/kg BW of ammonium acetate, and mice were injected with 10 mmol/kg BW. Increases in blood ammonia levels in rats 15-30 min after ammonia loading were prevented by treatment with 0.2 ml/100 g BW of biotin or 0.04 ml/100 g BW of arginine-glutamate with statistical significance. Blood ammonia levels after ammonia loading were lower, although not significantly, in the arginine glutamate-treated rats than in the biotin-treated animals. In mice also, increases in blood and brain ammonia levels after ammonia loading were prevented by the

administration of biotin. The decrease in brain glutamate and aspartate after ammonia loading was lower and the brain glutamine level was higher in biotin-treated mice than in the controls. These findings indicate the protective effect of biotin against ammonia intoxication.PMID: 7647902 [PubMed - indexed for MEDLINE]J Nutr 1997 Sep;127(9):1776-81 Related Articles, Books, LinkOut[Click here to read]Lipoic acid reduces the activities of biotin-dependent carboxylases in rat liver.Zempleni J, Trusty TA, Mock DM.Department of Pediatrics, University of Arkansas for Medical Sciences and the Arkansas Children's Hospital Research Institute, Little Rock, AR 72202, USA.In the past, lipoic acid has been administered to patients and test animals as therapy for diabetic neuropathy and various intoxications. Lipoic acid and the vitamin biotin have structural similarities. We sought to determine whether the chronic administration of lipoic acid affects the activities of biotin-dependent carboxylases. For 28 d, rats received daily intraperitoneal injections of one of the following: 1) a small dose of lipoic acid [4.3 micromol/( kg.d)]; 2) a large dose of lipoic acid [15.6 micromol/(kg.d)]; or 3) a large dose of lipoic acid plus biotin [15.6 and 2.0 micromol/(kg.d), respectively]. Another group received n-hexanoic acid [14.5 micromol/(kg.d)], which has structural similarities to lipoic acid and biotin and thus served as a control for the specificity of lipoic acid. A fifth group received phosphatidylcholine in saline injections and served as the vehicle control. The rat livers were assayed for the activities of acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and beta-methylcrotonyl-CoA carboxylase. Urine was analyzed for lipoic acid; serum was analyzed for indicators of liver damage and

metabolic aberrations. The mean activities of pyruvate carboxylase and beta-methylcrotonyl-CoA carboxylase were 28-36% lower in the lipoic acid-treated rats compared with vehicle controls (P < 0.05). Rats treated with lipoic acid plus biotin had normal carboxylase activities. Carboxylase activities in livers of n-hexanoic acid-treated rats were normal despite some evidence of liver injury. Propionyl-CoA carboxylase and acetyl-CoA carboxylase were not significantly affected by administration of lipoic acid. This study provides evidence consistent with the hypothesis that chronic administration of lipoic acid lowers the activities of pyruvate carboxylase and beta-methylcrotonyl-CoA carboxylase in vivo by competing with biotin.PMID: 9278559 [PubMed - indexed for MEDLINE]At 01:04 PM 1/19/2008, you wrote:>Hi ,>>I believe biotin can cause yeast die-off from what I've seen on the&g

t;other boards. we just started using it also.>>-- Internal Virus Database is out-of-date.Checked by AVG Free Edition. Version: 7.5.503 / Virus Database: 269.17.8/1196 - Release Date: 12/25/2007 12:18 PM

[Guest guest]

Alice,

I'm not really saying either, but just that people should know that the two

compete for transport, and actually, biotinidase and lipoamidase are the

same enzyme!

This would mean if you have problems with biotinidase, you probably also

have problems with lipoamidase and would need to supersupplement both!

I think when you are taking very high doses of one, maybe you should be

taking some level of the other....

1: Biochem J. 1993 Apr 15;291 ( Pt 2):545-51.

Co-purification of human serum lipoamidase and biotinidase: evidence that

the two

enzyme activities are due to the same enzyme protein.

Nilsson L, Kågedal B.

Department of Clinical Chemistry, University Hospital, Linköping, Sweden.

A more than 20000-fold purification of human serum lipoamidase is

described. This

was accomplished by (NH4)2SO4 precipitation and chromatography on

DEAE-Sepharose,

Blue Sepharose CL-6B and phenyl-Sepharose CL-4B, followed by preparative

isoelectric focusing (IEF) and finally by gel-permeation chromatography.

Co-precipitation and co-chromatography of lipoamidase and biotinidase

activities

with equal yields and purification were obtained in all the purification steps,

indicating that lipoamidase and biotinidase activities in human serum are

due to

the same enzyme protein. After preparative IEF, two fractions with both

lipoamidase activity and biotinidase activity were found at pI 4.0 and pI 4.4

respectively. The molecular mass of the enzyme was found to be 76 kDa. When

2-mercaptoethanol was used instead of cysteine as stabilizer during the

purification procedure, only one major form (pI 4.0) of the enzyme was obtained

after preparative IEF. By addition of cysteine, this form was transformed to an

enzyme with pI 4.4, indicating that this latter form is a cysteine adduct,

produced during the IEF procedure.

Publication Types:

Research Support, Non-U.S. Gov't

PMID: 8484735 [PubMed - indexed for MEDLINE]

2: Eur J Clin Chem Clin Biochem. 1992 Mar;30(3):119-26.

Lipoamidase and biotinidase deficiency: evidence that lipoamidase and

biotinidase

are the same enzyme in human serum.

Nilsson L, Ronge E.

Department of Clinical Chemistry, Faculty of Health Sciences, Linköping

University, Sweden.

Late-onset multiple carboxylase deficiency depends on biotinidase

deficiency and

is inherited as an autosomal recessive trait. Lipoamidase deficiency in humans

has not been previously reported, using the natural substrate lipoyllysine for

lipoamidase. In this report we describe a simultaneous decrease in both

lipoamidase and biotinidase activity in serum from a 21 month-old boy with a

profound biotinidase deficiency. Lipoamidase activity in human serum was

determined with both lipoyllysine (epsilon-N-(D,L-lipoyl)-L-lysine) and

N-D,L-lipoyl-p-aminobenzoate as substrates. Biotinidase activity was determined

with both biocytin (epsilon-N-(D-biotinyl-L-lysine) and

N-D-biotinyl-p-aminobenzoate as substrates. Our findings indicate that

lipoamidase activity and biotinidase activity in human serim are due to the

same

enzyme, but a " residual activity " was usually found when

N-D,L-lipoyl-p-aminobenzoate was used as a substrate. Compared with the

activity

in control serum, this " residual activity " was little affected by

inhibition with

biocytin, indicating that a small fraction of a modified biotinidase probably

exists.

Publication Types:

Research Support, Non-U.S. Gov't

PMID: 1599976 [PubMed - indexed for MEDLINE]

3: Clin Chim Acta. 1990 Aug 31;189(3):313-25.

Lipoamidase activity in human serum is due to biotinidase.

Garganta CL, Wolf B.

Department of Human Genetics, Medical College of Virginia, Richmond 23298.

Lipoamidase, as determined by lipoyl-p-aminobenzoic acid (L-pABA) hydrolyzing

activity, and biotinidase in human serum have similar pH profiles, molecular

weights, thermostabilities, and are similarly inhibited by

p-hydroxymercuribenzoate and not inhibited by phenylmethylsulfonylfluoride. A

monospecific polyclonal antibody prepared against biotinidase

immunoprecipitated

greater than 95% of serum L-pABA hydrolyzing activity and an identical

proportion

of biotinidase activity. In addition, children with profound biotinidase

deficiency (less than 10% normal serum activity) have greatly reduced levels of

L-pABA hydrolyzing activity in serum (less than 15% of mean normal

activity) and

obligate heterozygotes have activities intermediate between that of normal and

profoundly deficient individuals. These results indicate that most, if not all,

of the L-pABA hydrolyzing activity in human serum is due to biotinidase.

Moreover, since the Km of L-pABA hydrolysis by serum is high, it is

unlikely that

lipoic acid is recycled in the serum by biotinidase.

Publication Types:

Comparative Study

Research Support, U.S. Gov't, P.H.S.

PMID: 2225462 [PubMed - indexed for MEDLINE]

[]

>

--

Internal Virus Database is out-of-date.

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Version: 7.5.503 / Virus Database: 269.17.8/1196 - Release Date: 12/25/2007

12:18 PM