Synonymer & Anagram | Engelska ordet GLUTATHIONE


GLUTATHIONE

1
GSH

1

Antal bokstäver

11

Är palindrom

Nej

22
AT
ATH
GL
HI
IO
ION

1

9

12

AE
AEL
AEO
AET
AG


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Exempel på hur man kan använda GLUTATHIONE i en mening

  • Selenocysteine is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5′ deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases, selenophosphate synthetase 2, methionine-R-sulfoxide reductase B1 (SEPX1), and some hydrogenases).
  • As the precursor of other non-essential amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans.
  • The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water.
  • Kendall not only researched the adrenal glands, he also isolated thyroxine, a hormone of the thyroid gland and worked with the team that crystallized glutathione and identified its chemical structure.
  • Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec.
  • GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione as well as drug and xenobiotic detoxification.
  • The cause of biliary atresia in Egyptian infants has been proven to be as a result of aflatoxin induced cholangiopathy acquired prenatally in infants who have glutathione S transferase M1 deficiency.
  • Mechanisms for scavenging peroxyl radicals for the protection of cellular structures include endogenous antioxidants such as melatonin and glutathione, and dietary antioxidants such as mannitol and vitamin E.
  • Trypanothione is an unusual form of glutathione containing two molecules of glutathione joined by a spermidine (polyamine) linker.
  • Glutathione S-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification.
  • Thiols are generated when the amino acid cysteine and the peptide glutathione form strong complexes with methylmercury:.
  • Amino acids (300 mg glutamine; 200 mg arginine; 50 mg each asparagine, cystine, leucine, and isoleucine; 40 mg lysine hydrochloride; 30 mg serine; 20 mg each aspartic acid, glutamic acid, hydroxyproline, proline, threonine, tyrosine, and valine; 15 mg each histidine, methionine, and phenylalanine; 10 mg glycine; 5 mg tryptophan; and 1 mg reduced glutathione).
  • Other enzymes this may affect include, pyruvate dehydrogenase, citrate synthetase, malate dehydrogenase, glutathione reductase, and pyruvate decarboxylase.
  • Selenium and methionine also play separate roles in the formation and recycling of glutathione, a key endogenous antioxidant in many organisms, including humans.
  • This sudden surge of cytosolic hydrogen peroxide causes increased lipid peroxidation and additionally depletes ascorbate and glutathione stores.
  • In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH.
  • Homotetramers have four identical subunits (such as glutathione S-transferase), and heterotetramers are complexes of different subunits.
  • In addition to it, a rise in the activities of superoxide dismutase (SOD), chloramphenicol acetyltransferase (CAT), and glutathione S-transferase (GST) enzymes, in proportion to dose was seen in the rats, which were treated with BLCO for 21 days in a row.
  • Glutathione reacts with methylglyoxal to give a hemithioacetal, which converted into S--lactoyl-glutathione by glyoxalase I.
  • Mouth breathing as a result of decreased nasal breathing also increases lung surface exposure to irritants, pollutants, and allergens, causing neutrophilic inflammation in response to reactive oxygen species formation; research has found that individuals with genetically hindered glutathione counteraction of this oxidative stress are likely at a higher risk of developing EIB.


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