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"labile oxidase reaction"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
À̰ÍÀ» ¿øÇϼ̽À´Ï±î?
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  • ¿µ¹®
    ÇѱÛ
  • flocculation reaction
    ¼ØÅÐħÀü¹ÝÀÀ
  • foot placement reaction
    ¹ß³õ±â¹ÝÀÀ
  • footpad reaction
    ¹ß¹Ù´Ú¹ÝÀÀ
  • false negative reaction
    °ÅÁþÀ½¼º¹ÝÀÀ, °¡À½¼º¹ÝÀÀ
  • false positive reaction
    °ÅÁþ¾ç¼º¹ÝÀÀ, °¡¾ç¼º¹ÝÀÀ
  • fuchsin number reaction
    Ç«½Å¼ö¹ÝÀÀ
  • fuchsinophil reaction
    Ç«½Åģȭ¹ÝÀÀ
  • gel diffusion precipitin reaction
    °ÖÈ®»êħÀü¹ÝÀÀ
  • gluteal reaction
    º¼±â¹ÝÀÀ
  • graft versus host reaction
    ÀÌ½ÄÆí´ë¼÷ÁÖ¹ÝÀÀ
  • grief reaction
    ¾Öµµ¹ÝÀÀ
  • gross stress reaction
    ´ëÀڱعÝÀÀ, ÃÑüÀû½ºÆ®·¹½º¹ÝÀÀ
  • hyperkinetic reaction
    ¿îµ¿°ú´Ù¹ÝÀÀ
  • hypersensitivity reaction
    °ú¹Î¹ÝÀÀ
  • hypnic reaction
    ¼ö¸é¹ÝÀÀ
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  • ¿µ¹®
    ÇѱÛ
  • endothermic reaction
    Èí¿­¹ÝÀÀ
  • enzyme-antienzyme reaction
    È¿¼ÒÇ×È¿¼Ò¹ÝÀÀ
  • eosinophilic leukemoid reaction
    È£»ê±¸¹éÇ÷º´¸ð¾ç¹ÝÀÀ
  • equilibrium reaction
    ÆòÇü¹ÝÀÀ
  • erythrocyte sedimentation reaction
    ÀûÇ÷±¸Ä§°­¹ÝÀÀ
  • escape reaction
    µµÇǹÝÀÀ
  • exergonic reaction
    ¹ß¿­¹ÝÀÀ, ¿¡³ÊÁö¹æÃâ¹ÝÀÀ
  • exoergic reaction
    ¿ÜÀιÝÀÀ
  • exothermic reaction
    ¹ß¿­¹ÝÀÀ
  • explosive reaction
    Æø¹ß¹ÝÀÀ
  • false negative reaction
    °ÅÁþÀ½¼º¹ÝÀÀ
  • false positive reaction
    °ÅÁþ¾ç¼º¹ÝÀÀ
  • febrile transfusion reaction
    ¹ß¿­¼öÇ÷ºÎÀÛ¿ë
  • Fernandez reaction
    (¢¡lepromin test) ·¹ÇÁ·Î¹Î°Ë»ç
  • Feulgen¡¯s reaction
    Æ÷ÀϰչÝÀÀ
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  • ¿µ¹®
    ÇѱÛ
  • hysteric reaction
    È÷½ºÅ׸®¼º ¹ÝÀÀ
  • id reaction
    Id ¹ÝÀÀ
  • immune adherence reaction
    ¸é¿ªºÎÂø¹ÝÀÀ.
  • immune reaction
    ¸é¿ª¹ÝÀÀ.
  • immunologic reaction
    ¸é¿ª¹ÝÀÀ
  • immunological reaction
    ¸é¿ª¹ÝÀÀ.
  • immunoprecipitin reaction
    ¸é¿ªÄ§°­¹ÝÀÀ
  • indirect immunofluorescence reaction
    °£Á¢¸é¿ªÇü±¤¹ÝÀÀ.
  • indole reaction
    Àε¹¹ÝÀÀ.
  • indophenol reaction
    ÀεµÆä³î¹ÝÀÀ.
  • indophenol reaction
    ÀεµÆä³î¹ÝÀÀ
  • induced reaction
    À¯¹ß(µµ)¹ÝÀÀ.
  • inhibition reaction
    ¾ïÁ¦(¹ÝÀÀ), ÀúÁö(¹ÝÀÀ).
  • initial reaction
    Ãʱâ¹ÝÀÀ.
  • persistent light reaction
    Áö¼Ó¼º ±¤¹ÝÀÀ
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  • ¿µ¹®
    ÇѱÛ
  • biphasic reaction
    ÀÌ»ó¼º ¹ÝÀÀ(¡­Úãëë).
  • bisubstrate reaction
    µÎ±âÁú¹ÝÀÀ.
  • biuret reaction
    ºß·¿¹ÝÀÀ.
  • blanching reaction
    â¹é¹ÝÀÀ(¡­Úãëë)
  • blanching reaction
    â¹é¹ÝÀÀ(¡­Úãëë).
  • blood transfusion reaction
    ¼öÇ÷ºÎÀÛ¿ë.
  • cachexia reaction
    ¾Ç¾×Áú¼º ¹ÝÀÀ.
  • cadaveric reaction
    »çü¾ç¹ÝÀÀ (¡­åÆÚãëë).
  • cadmium reaction
    Ä«µå¹Å¹ÝÀÀ(¡­Úãëë).
  • capsular precipitation reaction
    Çù¸·Ä§°­¹ÝÀÀ
  • capsular swelling reaction
    Çù¸·ÆØÃ¢¹ÝÀÀ
  • carbazole reaction
    Ä«¸£¹ÙÁ¹¹ÝÀÀ(¡­Úãëë).
  • carbylamine reaction
    Ä«¸£ºô¾Æ¹Î¹ÝÀÀ.
  • cascade reaction
    ¿¬¼âÁõÆø¹ÝÀÀ
  • catalytic reaction
    Ã˸ŹÝÀÀ(¡­Úãëë).
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  • ¿µ¹®
    ÇѱÛ
  • photonuclear reaction
    ±¤ºØ±«¹ÝÀÀ(ÎÃÝÚÎÕÚãëë)
  • P-K reaction
    P-K ¹ÝÀÀ(Úãëë)
  • polymerase chain reaction
    ÁßÇÕÈ¿¼Ò ¿¬¼â¹ÝÀÀ(ñìùêý£áÈÖ§áðÚãëë)
  • Prausnitz-Kuestner reaction
    ÇÁ¶ó¿ì½º´ÏÃ÷-Å¥¿¡½ºÆ®³Ê ¹ÝÀÀ(Úãëë)
  • precipitin reaction
    ħ°­¼Ò(öØË½áÈ) ¹ÝÀÀ(Úãëë)
  • pseudounimolecular reaction
    À§´ÜºÐÀÚ¹ÝÀÀ(êÊÓ¤ÝÂí­Úãëë)
  • Quellung reaction
  • rapid reaction
    ±Þ¹ÝÀÀ(ÐáÚãëë)
  • reaction center
    ¹ÝÀÀ Áß½É(Úãëëñéãý)
  • reaction coordinate
    ¹ÝÀÀÁÂÇ¥(Úãëëñ¨øö)
  • reaction kinetics
    ¹ÝÀÀ ¼Óµµ·Ð(ÚãëëáÜÓøÖå)
  • reaction mixture
    ¹ÝÀÀ È¥ÇÕ¹°(ÚãëëûèùêÚª)
  • reaction of identity
    µ¿Áú¼º ¹ÝÀÀ(ÔÒòõàõÚãëë)
  • reaction of nonidentity
    ÀÌÁú¼º ¹ÝÀÀ(ì¶òõàõÚãëë)
  • reaction of partial identity
    ºÎºÐ µ¿Áú¼º(Ý»ÝÂÔÒòõàõ) ¹ÝÀÀ(Úãëë)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 8
CPRO coproporphyrinogen oxidase
DAAO diaminoacid oxidase
DAO diamine oxidase
DO Doctor of Osteopathy (one of two fully recognized medical practioners in the US-the other being MD);...
dopase dihydroxyphenylalanine oxidase
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 8
XOD HPX)-xanthine oxidase
XO HX)-xanthine oxidase
HX/XO Hypoxanthine/xanthine oxidase
LAO L-Amino acid oxidase
LO Lysyl oxidase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 8
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • reaction
    ¹ÝÀÀ
  • reaction formation
    ¹Ýµ¿ Çü¼º
    ¾ïÁ¦µÈ ¹Ý»çȸÀûÀÎ Ãæµ¿°ú´Â »ó¹ÝµÇ°í ¶ÇÇÑ ±×°ÍÀÇ ´ë½ÅÀÌ µÇ´Â ¾î¶² ŵµ¸¦ ¹«ÀǽÄÀûÀ¸·Î ÃëÇÏ°Ô µÇ´Â Á¤½Å ±â±¸.
  • reaction of identity
    ÀÏÄ¡ ¹ÝÀÀ
  • reaction of partial identity
    ºÎºÐ ÀÏÄ¡ ¹ÝÀÀ
  • reaction threshold
    ¹ÝÀÀ ¿ªÄ¡
    ÀÚ±ØÀ» ÁØ ÈÄ ¹ÝÀÀÀÌ ÀϾ±â±îÁöÀÇ °ª.
  • reversible reaction
    °¡¿ª ¹ÝÀÀ
  • scratch reaction
    ¼ÒÆÄ ¹ÝÀÀ
    Áï½ÃÇü ¾Ë·¯Áö ÁúȯÀÇ Áø´Ü¹ý.
  • serologic reaction
    Ç÷û ¹ÝÀÀ, Ç÷ûÇÐÀû ¹ÝÀÀ
  • serum colloidal reaction
    Ç÷û ±³Áú ¹ÝÀÀ
    °£ ±â´É °Ë»çÀÇ Á¾·ù.
  • serum reaction
    Ç÷û ¹ÝÀÀ
    Ç׿ø Ç×ü ¹ÝÀÀÀ» ½ÃÇè°ü ³»¿¡¼­ ÀçÇöÇÒ ¼ö ÀÖ´Â ¹ÝÀÀ.
  • shock circuit reaction
    ´Ü¶ô ¹ÝÀÀ
    °¨Á¤Àû Ãæµ¿ÀÌ À̼ºÀÇ ÅëÁ¦¸¦ ¹þ¾î³ª Á÷Á¢À¸·Î Çൿ¿¡ ¿Å°ÜÁö´Â ¹ÝÀÀ.
  • side reaction
    ºÎÀÛ¿ë, ºÎ¹ÝÀÀ
  • skin reaction
    ÇǺΠ¹ÝÀÀ
  • successive reaction
    ¹Ýº¹ ¹ÝÀÀ
  • toxic reaction
    µ¶ ¹ÝÀÀ, Áßµ¶ ¹ÝÀÀ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 8
d-amino-acid oxidase <enzyme> Chemical name: D-Amino-acid:oxygen oxidoreductase (deaminating)
Registry number: EC 1.4.3.3
(12 Dec 1998)
sulochrin oxidase <enzyme> Fungal enzyme converts sulochrin to bisdechlorogeodin
Registry number: EC 1.1.-
(26 Jun 1999)
D-arabinonolactone oxidase <enzyme> From candida albicans atcc 10231; catalyses the biosynthesis of d-erythro-ascorbic acid from d-arabinono-1,4-lactone
Registry number: EC 1.1.3.-
Synonym: d-arabinono-1,4-lactone oxidase
(26 Jun 1999)
diamine oxidase amine oxidase (copper-containing), amine oxidase (flavin-containing)
dicarboxylic acid-CoA oxidase <enzyme> Oxidises dicarboxylic acid CoA esters using molecular oxygen and producing hydrogen peroxide, ultimately producing a dicarboxylic acid with 2 fewer carbon atoms
Registry number: EC 1.3.3.-
Synonym: dicarboxylyl-CoA oxidase, dicarboxylic acid-coenzyme a oxidase
(26 Jun 1999)
dihdroxyindole-carboxylic acid oxidase <enzyme> Converts 5,6-dihydroxyindole-2-carboxylic acid to melanochrome in premelanosomes; no further information on mechanism 6/95
Registry number: EC 1.-
Synonym: dhica oxidase, dhi2c oxidase
(26 Jun 1999)
dihydrobenzophenanthridine oxidase <enzyme> Copper-containing oxidase from sanguinaria canadensis; converts dihydrophenanthridines to the corresponding alkaloids, sanguinarine or chelerythrine; requires oxygen, does not contain flavins or pyridine nucleotides; inhibited by thiols
Registry number: EC 1.3.3.-
Synonym: dihydrosanguinarine oxidase, dihydronorsanguinarine oxidase, dihydrochelerythrine oxidase
(26 Jun 1999)
dihydrogeodin oxidase <enzyme> Copper-containing enzyme which converts dihydrogeodin to (+)-geodin by an intramolecular phenol oxidative coupling reaction; isolated from aspergillus terreus
Registry number: EC 1.10.3.-
(26 Jun 1999)
dihydroorotate oxidase <enzyme> An enzyme that in the course of pyrimidine biosynthesis, catalyses the oxidation of dihydro-orotic acid to orotic acid utilizing oxygen as the electron acceptor. This enzyme is a flavoprotein which contains both fad and fmn as well as iron-sulfur centres.
Chemical name: (S)-Dihydroorotate:oxygen oxidoreductase
Registry number: EC 1.3.3.1
(12 Dec 1998)
dihydropterin oxidase <enzyme> From drosophila melanogaster; uses a variety of 2-amino-4-oxo-7,8-dihydropteridine cpds as substrates; during reaction 1 mole of molecular o2 is consumed/mole substrate oxidised producing h2o2
Registry number: EC 1.5.3.-
(26 Jun 1999)
dihydrouracil oxidase <enzyme> Oxygen dependent; no cofactor required, forms uracil irreversibly; enzyme from rhodosporidium toruloides
Registry number: EC 1.3.3.-
(26 Jun 1999)
diphenol oxidase <enzyme> An enzyme of the oxidoreductase class that catalyses the reaction between catechol and oxygen to yield benzoquinone and water. It is a complex of copper-containing proteins that acts also on a variety of substituted catechols.
Chemical name: 1,2-Benzenediol:oxygen oxidoreductase
Registry number: EC 1.10.3.1
(12 Dec 1998)
dopa oxidase Provisional name given the enzyme(s) catalyzing the formation of melanins from dopa; it now appears that the copper-containing monophenol monooxygenases and/or catechol oxidases are responsible for the oxidation of l-tyrosine to dopa and dopa quinone.
(05 Mar 2000)
duroquinol oxidase <enzyme> Consists of fixn, fixo, and fixp proteins in bradyrhizobium, in which fixo and fixp are c-type cytochromes; does not contain cytochromes, probably a flavoprotein; a proto-haem containing oxidase expressed by the cyoabc locus in paracoccus denitrificans
Registry number: EC 1.-
Synonym: aroid alternative oxidase, quinol oxidase, trypanosoma alternative oxidase, cyanide-resistant alternative oxidase, cytochrome bb3, cytochrome bb(3)
(26 Jun 1999)
indole-3-ethanol oxidase <enzyme> Involved in conversion of indole-3-ethanol to indole-3-acetic acid; isolated from seeds of the bean phaseolus vulgaris; not stimulated by nadp or fad; do not confuse with nad- or nadp-dependent indole-3-ethanol oxidases
Registry number: EC 1.1.-
Synonym: tryptophol oxidase
(26 Jun 1999)
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