PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “THIAMINE PYROPHOSPHATE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,009 records · Page 56Linked to original sources
PubMed1993

Kinetics of thiamin and thiamin phosphate esters in human blood, plasma and urine after 50 mg intravenously or orally.

The concentrations of thiamin and thiamin monophosphate and diphosphate in plasma and whole blood samples were assessed in six healthy subjects for 12 h and in urine for 24 h following an IV and PO bolus dose of 50 mg thiamin HCl. Unphosphorylated thiamin increased rapidly in plasma after IV administration and then decreased to its initial value within 12 h in all but one subject; the half-life was 96 min. Thiamin mono and -diphosphate increased moderately (56%), and decreased slowly; the half-life of diphosphate was 664 min. Within 24 h, 53% of the administered dose was recovered in the urine, indicating a restricted distribution. After oral administration, the peak thiamin concentration in plasma was reached after 53 min and the concentration then had increased to 179% of its initial value. The elimination half-life was 154 min, and only 2.5% of the given dose was recovered in the urine. The relative bioavailability of thiamin was 5.3%. A moderate amount of the administered thiamin was stored in blood. Other body tissues must play an important part, therefore, in the distribution of thiamin.

Administration, Oral↗
PubMed1979

Biochemical assessment of thiamine nutrition in childhood.

The activity of red cell transketolase and TPP-effect were determined in 1028 infants and children, aged 1 month to 14 years, using a micromethod. All the children were healthy and without evidence of malnutrition. Transketolase activity decreased in the second year of life, followed by a constant increase up to the 6th year. Activity did not change in the next four years, then a steady decrease occurred. TPP-effect was not as stable as transketolase activity, and decreased significantly from years 3 to 5 and increased significantly from years 5 to 7. Beginning with year 10, TPP-effect decreased gradually. 6.6% of all children investigated had marginally deficient TPP-effects and 1.3% were biochemically deficient without clinical signs of avitaminosis. A group of 37 adults had transketolase activities and TPP-effect comparable to those of the 13 year-olds. Effect appeared to be marginal in 5.4% and deficient in 2.7%.

Adolescent↗
PubMed1978

Congenital lactic acidosis due to pyruvate carboxylase deficiency: absence of an inhibitor of TPP-ATP phosphoryl transferase.

Two children are described who suffered from episodes of metabolic acidosis and progressive mental and motor deterioration. The patients showed periodic elevation of blood lactate, pyruvate and alanine, which was accompanied by vomiting, hypotonia or convulsions. The concentrations of lactate and pyruvate in cerebrospinal fluid were found to be increased. Liver biopsies revealed a decrease in pyruvate carboxylase activity and normal pyruvate decarboxylase activity. No inhibitor of TPP-ATP phosphoryl transferase was detected in urine from the patients. These findings suggest that congenital lactic acidosis due to pyruvate carboxylase deficiency is probably a different disease entity from Leigh's encephalomyelopathy. A possible mechanism of brain damage caused by a defect in pyruvate carboxylase is postulated.

Acidosis↗
PubMed1975

The active species of "CO2" utilized in ferredoxin-linked carboxylation reactions.

The active species of "CO2", i.e. CO2 or HCO-3(H2CO3) utilized by enzymes catalyzing ferredoxin-linked carboxylation reactions was determined. The enzyme investigated was pyruvate synthase from Clostridium pasteurianum (EC 1.2.7.1; Pyruvate: ferredoxin oxidoreductase). Data were obtained which were compatible with those expected if CO2 is the active species. The dissociation constant (Ks) of the enzyme-CO2 complex was measured. At pH 7.2 Ks for CO2 of pyruvate synthase was found to be approximately 5 mM.

Acetyl Coenzyme A↗