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"pyruvate oxidation factor"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • complementary factor
    º¸ÃæÀÎÀÚ
  • conglutinogen activating factor
    ±³Âø¿øÈ°¼ºÀÎÀÚ
  • conversion factor
    º¯È¯ÀÎÀÚ, º¯È¯°è¼ö
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ
  • corticotropin-releasing factor
    ºÎ½Å°ÑÁúÀÚ±ØÈ£¸£¸ó¹æÃâÀÎÀÚ
  • chemotactic factor
    È­Çнò¸²ÀÎÀÚ
  • drug resistance factor
    ¾àÁ¦ÀúÇ×ÀÎÀÚ
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢º´À¯¹ßÀÎÀÚ
  • decay accelerating factor
    ºØ±«ÃËÁøÀÎÀÚ
  • dilution factor
    Èñ¼®ÀÎÀÚ
  • exclusion of confounding factor
    ±³¶õ¹èÁ¦ÀÎÀÚ
  • exogenous factor
    ¿ÜÀοä¼Ò
  • extrinsic factor
    ¿ÜÀÎÀÎÀÚ, ¿ÜÀÎÀÚ
  • elongation factor
    ´ÃÀÓÀÎÀÚ, ¿¬ÀåÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • common factor
    °øÅëÀÎÀÚ
  • competence factor
    Àû°ÝÀÎÀÚ
  • competence inducing factor
    Àû°ÝÀ¯¹ßÀÎÀÚ
  • complementary factor
    º¸ÃæÀÎÀÚ, º¸Ã¼ÀÎÀÚ
  • conglutinogen activating factor
    ±³Âø¿øÈ°¼ºÀÎÀÚ
  • conversion factor
    º¯È¯ÀÎÀÚ, º¯È¯°è¼ö
  • corticotropin releasing factor
    ºÎ½Å°ÑÁúÀÚ±ØÈ£¸£¸ó¹æÃâÀÎÀÚ
  • decay accelerating factor
    ºØ±«ÃËÁøÀÎÀÚ
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢À¯¹ßÀÎÀÚ
  • dilution factor
    ¹±ÈûÀÎÀÚ, Èñ¼®ÀÎÀÚ
  • drug resistance factor
    ¾àÁ¦ÀúÇ×ÀÎÀÚ
  • elongation factor
    ´ÃÀÓÀÎÀÚ, ¿¬ÀåÀÎÀÚ
  • endothelium-derived contracting factor
    ³»ÇǼ¼Æ÷¼öÃàÀÎÀÚ
  • endothelium-derived relaxing factor
    ³»ÇǼ¼Æ÷ÀÌ¿ÏÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • Fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷(àéë«Ù½á¬øà)¼ºÀå¿äÀÎ(à÷íþé©ì×)
  • G-CSF (Granulocyte colony-stimulating factor)
    °ú¸³¼¼Æ÷±ºÃËÁøÀÎÀÚ(Î¨Ø£á¬øàÏØõµòäì×í­)
  • GH releasing factor
    ¼ºÀå(à÷íþ)È£¸£¸ó À¯¸®ÀÎÀÚ(ë´×îì×í­).
  • GH releasing factor
    ¼ºÀåÈ£¸£¸óÀ¯¸®ÀÎÀÚ.
  • Growth factor
    ¼ºÀåÀÎÀÚ(à÷íþì×í­)
  • Hageman factor
    ÇϰԸ¸ÀÎÀÚ
  • Hydrostatic factor
    Á¤¼öÀÎÀÚ(ð¡â©ì×í­)
  • IGF-I(insulin-like growth factor-I)
    Àν¶¸° À¯»ç ¼ºÀåÀÎÀÚ-1
  • Luteinization -inhibiting factor
    Ȳüȭ¾ïÁ¦¿äÀÎ(üÜô÷ûùåäð¤é©ì×)
  • Macrophage colony-stimulating factor
    ´ë½Ä¼¼Æ÷Áý¶ôÇü¼ºÃËÁøÀÎÀÚ(ÓÞãÝá¬øàó¢Õªû¡à÷õµòäì×í­)à÷õµòäì×?
  • NGF=>nerve growth factor
    ½Å°æ¼ºÀåÀÎÀÚ
  • PAF =platelet activating factor
    Ç÷¼ÒÆÇȰ¼ºÀÎÀÚ.
  • PAF= platelet activating factor
    Ç÷¼ÒÆÇ Ȱ¼ºÀÎÀÚ.
  • Q factor
    Å¥ ÀÎÀÚ
  • Q-factor
    Å¥-ÀÎÀÚ (ì×í­)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • time, dose and fractionation factor, TDF factor
    ½Ã°£¼±·®ºÐÇÒÀÎÀÚ
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • age factor
    ¿¬·ÉÀÎÀÚ.
  • air kerma calibration factor
    °ø±âÄ¿¸¶ÃøÁ¤°è¼ö, -´«±Ý¸ÂÃã°è¼ö
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ(¡­ýüà·ì×í­).
  • amplification factor
    ÁõÆøÀÎÀÚ
  • anisotropy factor
    ºñµî¹æ¼º°è¼ö
  • antigen, colonization factor
    Áý¶ôÇü¼ºÀÎÀÚÇ׿ø, ¼¼Æ÷±ºÇü¼ºÀÎÀÚÇ׿ø
  • antihemophilic A factor =AHA
    Ç×Ç÷¿ìº´ AÀÎÀÚ(?ËöËö).
  • antihemophilic factor =AHF
    Ç×Ç÷¿ìº´ÀÎÀÚ(¡­ì×í­)
  • antihemophilic factor =AHF
    Ç×Ç÷¿ìº´ÀÎÀÚ(?ËöËö).
  • antihemophllic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antiinsulin factor
    Ç×Àν¶¸°ÀÎÀÚ.
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ(ù÷ãêÌèæúì×í­).
  • antinuclear factor =ANF
    Ç×ÇÙÀÎÀÚ.
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  • ¿µ¹®
    ÇѱÛ
  • anti-fatty-liver-factor
    Ç×Áö¹æ°£ÀÎÀÚ(ù÷ò·Û¸ÊÜì×í­)
  • anti-gray-hair factor
    Ç×¹é¸ð¹ß ÀÎÀÚ(ù÷ÛÜÙ¾Û¥ì×í­)
  • antiacrodynia factor
    Ç×Áö´Üµ¿Åë ÀÎÀÚ(ù÷ò¶Ó®ÔÙ÷Ôì×í­)
  • antianemia factor
    Ç׺óÇ÷ÀÎÀÚ(ù÷Þ¸úìì×í­)
  • antiberiberi factor
    Ç×°¢±âÀÎÀÚ(ù÷ÊÅѨì×í­)
  • antiblack-tongue factor
    Ç×Èæ¼³ÀÎÀÚ(ù÷ýÙàßì×í­)
  • antihemophilic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ(ù÷úìéÒÜ»ì×í­)
  • antihemophilic factor B
    Ç×Ç÷¿ìº´ÀÎÀÚ (ù÷úìéÒÜ»ì×í­) B
  • antihemophilic factor C
    Ç×Ç÷¿ìº´ÀÎÀÚ (ù÷úìéÒÜ»ì×í­) C
  • antineuritic factor
    Ç׽Ű漺ÀÎÀÚ(ù÷ãêÌèàõì×í­)
  • antinuclear factor
    Ç×ÇÙÀÎÀÚ(ù÷ú·ì×í­)
  • antipellagra factor
    Ç×(ù÷)Æç¶ó±×¶ó ÀÎÀÚ(ì×í­)
  • antipeptic ulcer factor
    Ç×(ù÷)±Ë¾ç(Ï÷åË) ÀÎÀÚ(ì×í­)
  • antipernicious anemia factor
    Ç×(ù÷)¾Ç¼ººóÇ÷(äÂàõÞ¸úì) ÀÎÀÚ(ì×í­)
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ(ù÷ÎÕúìÜ»ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
LPF leukocytosis-promoting factor; leukopenia factor; lipopolysaccharide factor; localized plaque format...
MIF macrophage inhibitory factor; melanocyte[-stimulating hormone]-inhibiting factor; maximum inspirator...
MRF Markov random field; medical record file; melanocyte-[stimulating hormone]-releasing factor; mesence...
NF nafcillin; National Formulary; nephritic factor; neurofibromatosis; neurofilament; neutral fraction;...
RF radial fiber; radio frequency; receptive field; regurgitant fraction; Reitland-Franklin [unit]; rela...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
GPT Glutamic-pyruvate transaminase
LPK L Pyruvate kinase
P L)-pyruvate
L/P Lactate/pyruvate
P-pyruvate Phosphoenolpyruvate
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • bone factor
    °ñ ÀÎÀÚ
    Ȱ¼ºÀ̳ª ÀÚÁï¿¡ ´ëÇÑ Ä¡Á¶°ñÀÇ »ó´ë ¹ÝÀÀ.
  • Castle factor
    ij½½ ÀÎÀÚ
    ½ÄǰÀ̳ª À§¾× ¼Ó¿¡ ÀÖ´Â Ç׺óÇ÷ ÀÎÀÚ. À̰ÍÀÌ °áÇÌµÇ¸é ¾Ç¼º ºóÇ÷ÀÌ µÈ´Ù. À§¾×¿¡ ÇÔÀ¯µÈ ij½½³» ÀÎÀÚ¿Í ½Äǰ¿¡ ÇÔÀ¯µÈ ij½½¿Ü ÀÎÀÚ°¡ ÀÖ´Ù. ³»ÀÎÀÚ°¡ °áÇÌµÇ¸é ½Äǰ ³»ÀÇ ¿ÜÀÎÀÚ°¡ Èí¼öµÇÁö ¾Ê°í ¾Ç¼º ºóÇ÷ÀÌ ÀϾ´Ù. À§ ¾Ï µîÀ¸·Î À§¸¦ ÀüºÎ Àß¶ó¹ö¸®¸é ºóÇ÷ÀÌ ÀϾ´Â °ÍÀº ³»ÀÎÀÚ°¡ ¾ø¾îÁö±â ¶§¹®ÀÌ´Ù. ³»ÀÎÀÚ´Â ºÐÀÚ·® ¾à 10¸¸ÀÎ ´Ü¹éÁú·Î À§º®ÀÇ ¹æ ¼¼Æ÷¿¡¼­ ºÐºñµÈ´Ù. ¿ÜÀÎÀڷμ­´Â ºñŸ¹Î D°¡ °ü°èÇÑ´Ù. 1927³â ¹Ì±¹ÀÇ W.B. ij½½ÀÌ Ã³À½À¸·Î ÀÌ·¯ÇÑ ±¸Á¶¸¦ Á¦Ã¢ÇÏ¿´´Ù.
  • Castles extrinsic factor
    ij½½ ¿ÜÀÎÀÚ
  • cavity-gas calibration factor
    °­-±âü ±³Á¤ °è¼ö
  • certainty factor
    È®½Ç ¿äÀÎ
  • chamber calibration factor
    Àü¸®ÇÔ ÃøÁ¤ °è¼ö, »óÀÚ ÃøÁ¤ °è¼ö
  • circumstance factor
    »óȲ ÀÎÀÚ
  • clotting factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • clumping factor
    ÀÀ±« ÀÎÀÚ
  • coagulase-reacting factor
    Ç÷Àå ÀÀ°í È¿¼Ò ¹ÝÀÀ ÀÎÀÚ
  • coagulation factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°í ÀÎÀÚ ¾ïÁ¦Á¦
  • colicin factor
    Äݸ®½Å ÀÎÀÚ
  • colony stimulating factor
    ±ºÃ¼ ÀÚ±Ø ¿ä¼Ò, Áý¶ô ÀÚ±Ø ÀÎÀÚ
    ¹ß´Þ ´Ü°èÀÇ Àü±¸Àû ¼¼Æ÷°¡ Áý¶ôÀ» Çü¼ºÇÏ´Â °úÁ¤¿¡´Â À̰ÍÀÇ ÀÛ¿ëÀÌ ÇÊ¿äÇÏ´Ù´Â °ÍÀÌ ÀνĵǾú´Ù. ÀÌ ÀÎÀÚ´Â ¼¶À¯¾Æ¼¼Æ÷, ³»ÇǼ¼Æ÷, ´ë½Ä¼¼Æ÷ µî¿¡¼­ »ý»êµÇ¸ç ¼º¼÷ÇÑ ¸é¿ª°è ¼¼Æ÷ÀÇ ÀÛ¿ë¿¡µµ ¿µÇâÀ» ³¢Ä£´Ù.
  • competence inducing factor
    Àû°Ý À¯¹ß ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
pyruvate carboxylase <enzyme> An enzyme that catalyses the formation of oxaloacetate from pyruvate, carbon dioxide and ATP in gluconeogenesis.
(18 Nov 1997)
pyruvate carboxylase deficiency An autosomal recessive pyruvate metabolism disorder resulting from absent or deficient expression of pyruvate carboxylase activity. Decreased production of oxaloacetate leads to decreased gluconeogenesis, thereby causing fasting hypoglycaemia, lactic acid acidosis, and decreased synthesis of amino acid neurotransmitters. Clinical presentations include acidosis, ataxia, mental retardation; sometimes co-occurs with leigh disease.
(12 Dec 1998)
pyruvate decarboxylase <enzyme> Catalyses the decarboxylation of an alpha keto acid to an aldehyde and carbon dioxide. Thiamine pyrophosphate is an essential cofactor. In lower organisms, which ferment glucose to ethanol and carbon dioxide, the enzyme irreversibly decarboxylates pyruvate to acetaldehyde.
Registry number: EC 4.1.1.1
(12 Dec 1998)
pyruvate dehydrogenase <enzyme> A complex multienzyme system that catalyses the conversion of (pyruvate + CoA + NAD) to (acetyl CoA + CO2 + NAD).
(18 Nov 1997)
pyruvate dehydrogenase complex <enzyme> A complex multienzyme system that catalyses the conversion of (pyruvate + CoA + NAD) to (acetyl CoA + CO2 + NAD).
(18 Nov 1997)
pyruvate dehydrogenase complex deficiency An autosomal recessive pyruvate metabolism disorder resulting from deficient enzyme activity in one of several proteins of pyruvate dehydrogenase complex, resulting in deficiency of acetyl CoA. Deficiency in acetyl CoA product reduces the synthesis of acetylcholine, thereby causing neurological abnormalities. Clinical presentations include lactic acidosis, mental retardation, and ataxia.
(12 Dec 1998)
pyruvate dehydrogenase complex inactivase <enzyme> Pharmacological action: enzyme inhibitor
Registry number: EC 3.4.-
(26 Jun 1999)
pyruvate dehydrogenase (cytochrome) An oxidoreductase catalyzing reaction between ferricytochrome b1 and pyruvate to yield acetate and CO2, and ferrocytochrome b1.
(05 Mar 2000)
pyruvate dehydrogenase (lipoamide) An oxidoreductase catalyzing conversion of pyruvate and (oxidised) lipoamide to CO2 and S6-acetyldihydrolipoamide in two successive reactions: the first between pyruvate and thiamin pyrophosphate to yield CO2 and alpha-hydroxyethylthiamin pyrophosphate (active pyruvate); the second between the last named and lipoamide to regain the thiamin pyrophosphate and yield S6-acetylhydrolipoamide.
Compare: alpha-ketodecarboxylase.
(05 Mar 2000)
pyruvate dehydrogenase (lipoamide)-phosphatase <enzyme> (pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyses the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex.
Registry number: EC 3.1.3.43
(12 Dec 1998)
pyruvate-formate-lyase-deactivase <chemical> Encoded by adhe gene product from E coli; pfla (radical form) yields pfl (non-radical form) in presence of fe++, nad and CoA and the multienzyme complex consisting of alcohol plus acetaldehyde-CoA dehydrogenase activities
Synonym: pfl-deactivase, adhe multienzyme, adhe gene product
(26 Jun 1999)
pyruvate kinase <enzyme> ATP:pyruvate 2-o-phosphotransferase. A phosphotransferase that catalyses reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (l, r, m1, and m2). Deficiency of the enzyme results in haemolytic anaemia.
Registry number: EC 2.7.1.40
(12 Dec 1998)
pyruvate kinase deficiency A disorder in which there is a deficiency of pyruvate kinase in red blood cells; characterised by haemolytic anaemia varying in degree from one patient to another; autosomal recessive inheritance.
(05 Mar 2000)
pyruvate kinase phosphatase <enzyme> Reactivates pyruvate kinase
Registry number: EC 3.1.3.-
(26 Jun 1999)
pyruvate metabolism, inborn errors Hereditary disorders of pyruvate metabolism. They are difficult to diagnose and describe because pyruvate is a key intermediate in glycolysis, gluconeogenesis, and the tricarboxylic acid cycle. Some inherited metabolic disorders may alter pyruvate metabolism indirectly. Disorders in pyruvate metabolism appear to lead to deficiencies in neurotransmitter synthesis and, consequently, to nervous system disorders.
(12 Dec 1998)
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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  • Á¦Ç°¸í
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    ±¸ºÐ/º¸Çè±Þ¿©
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    ÇѱÛ
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    ÇѱÛ
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KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 3
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