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"DIS2 protein phosphatase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • human plasma protein fraction
    »ç¶÷Ç÷Àå´Ü¹éºÐÀ²
  • iron binding protein
    ö°áÇմܹéÁú
  • major basic protein
    ÁÖ¿ä±âÃʴܹéÁú, ÁÖ±âÀú´Ü¹éÁú
  • mitogen-activated protein kinase
    ¹ÌÅä°ÕȰ¼ºÈ­´Ü¹éÁúŰ³ª¾ÆÁ¦
  • monocyte chemotactant protein
    ´ÜÇÙ±¸È­Çнò¸²´Ü¹éÁú, ´ÜÇÙ±¸È­ÇÐÁÖ¼º´Ü¹é
  • matrix protein
    ¹ÙÅÁÁú´Ü¹éÁú
  • membrane control protein
    ¸·Á¶Àý´Ü¹éÁú
  • olfactory binding protein
    Èİ¢°áÇմܹéÁú
  • oligomeric protein
    ¿Ã¸®°í¸Ó´Ü¹éÁú
  • principal outer membrane protein
    ÁÖ¹Ù±ù¸·´Ü¹éÁú, Áֿܸ·´Ü¹éÁú
  • prosthetic protein
    ¹èÇմܹéÁú
  • protein
    ´Ü¹éÁú
  • protein binding
    ´Ü¹éÁú°áÇÕ
  • protein bound iodine
    ´Ü¹éÁú°áÇÕ¿ä¿Àµå
  • protein granule
    ´Ü¹éÁú°ú¸³
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  • ¿µ¹®
    ÇѱÛ
  • protein kinase
    ´Ü¹éÁúŰ³ª¾ÆÁ¦
  • protein layer
    ´Ü¹éÁúÃþ
  • major basic protein
    ÁÖ±âÀú´Ü¹é, ÁÖ¿ä±âÃʴܹé
  • matrix protein
    ¹ÙÅÁÁú´Ü¹é
  • membrane control protein
    ¸·Á¶Àý´Ü¹é
  • monocyte chemotactant protein
    ´ÜÇÙ±¸È­Çнò¸²´Ü¹é, ´ÜÇÙ±¸È­ÇÐÁÖ¼º´Ü¹é
  • olfactory binding protein
    Èİ¢°áÇմܹé
  • oligomeric protein
    ¿Ã¸®°í¸Ó´Ü¹éÁú
  • protein
    ´Ü¹é, ´Ü¹éÁú
  • principal outer membrane protein
    Áֿܸ·´Ü¹éÁú
  • prosthetic protein
    ¹èÇմܹé
  • protein quotient
    ´Ü¹éÁö¼ö
  • protein score
    ´Ü¹é°¡
  • protein sensitization
    ´Ü¹é¹Î°¨
  • reserve protein
    ÀúÀå´Ü¹éÁú
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  • ¿µ¹®
    ÇѱÛ
  • M protein
    M´Ü¹éÁú
  • M protein
    M´Ü¹é.
  • NPN= non protein nitrogen
    ºñ´Ü¹éÁú¼Ò.
  • POMP (principal outer membrane protein)
    ÁÖ¿ä¿Ü¸·´Ü¹éÁú
  • PPD (purified protein derivatives)
    ÇÇÇǵð, Á¤Á¦´Ü¹éÁú·ù(À¯µµÃ¼)
  • PPD(Purified protein derivative) test
    PPD °Ë»ç.
  • Reiters protein
    ¶óÀÌÅÍ ¸Åµ¶Áø´Ü¿ë´Ü¹éÁú
  • S100 protein
    S100 ´Ü¹éÁú
  • actin-binding protein
    ¾×ƾ °áÇմܹé(¡­Ì¿ùêÓ±ÛÜ)
  • activated protein C inhibitor
    Ȱ¼ºÈ­´Ü¹éÁú C ¾ïÁ¦Á¦
  • activated protein C resistance
    Ȱ¼ºÈ­C´Ü¹é³»¼º
  • acute phase protein
    ±Þ¼ºº´±â´Ü¹éÁú
  • acute phase reactive protein
    ±Þ¼º±â ¹ÝÀÀ¼º ´Ü¹é.
  • amyloid precurssor protein
    ¾Æ¹Ð·ÎÀ̵å Àü±¸ ´Ü¹éÁú
  • androgen- binding protein
    ¸¸¼ºÈ£¸£¸ó °áÇմܹé
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  • ¿µ¹®
    ÇѱÛ
  • activated protein C inhibitor
    Ȱ¼ºÈ­´Ü¹éÁú C ¾ïÁ¦Á¦
  • activated protein C resistance
    Ȱ¼ºÈ­C´Ü¹é³»¼º
  • acute phase protein
    ±Þ¼ºº´±â´Ü¹éÁú
  • acute phase reactive protein
    ±Þ¼º±â ¹ÝÀÀ¼º ´Ü¹é.
  • al protein
    AL ´Ü¹é(¡­Ó±ÛÜ)
  • amyloid precurssor protein
    ¾Æ¹Ð·ÎÀ̵å Àü±¸ ´Ü¹éÁú
  • androgen- binding protein
    ¸¸¼ºÈ£¸£¸ó °áÇմܹé
  • anion exchange protein
    À½À̿ ±³È¯ ´Ü¹é(ÎßüµÓ±ÛÜ)
  • antifreeze protein
    Ç×µ¿°á´Ü¹éÁú(ù÷ÔÐÌ¿ Ó±ÛÜòõ).
  • bacterial cell protein
    ±Õü´Ü¹é(Áú).
  • bactericidal permeability increasing protein(bpip)
    Bactericidal permeability increasing protein
  • bence-jones protein
    º¥½º-Á¸½º ´Ü¹é(¡­Ó±ÛÜ)
  • blood protein
    Ç÷¾×´Ü¹é(¡­Ó±ÛÜ).
  • body protein
    ü´Ü¹é(Áú)(ô÷Ó±ÛÜòõ).
  • c-Jun protein
    ¾¾-ÁØ ´Ü¹é(Ó±ÛÜ)
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  • ¿µ¹®
    ÇѱÛ
  • carboxyl carrier protein
    Ä«¸£º¹½Ç ¿î¹Ý´Ü¹éÁú(ê¡ÚæÓ±ÛÜòõ)
  • carrier protein
    ¿î¹Ýü´Ü¹éÁú(ê¡Úæô÷Ó±ÛÜòõ)
  • catabolite activator protein
    īŸº¼¶óÀÌÆ® Ȱ¼ºÈ­ ´Ü¹éÁú(üÀàõûùÓ±ÛÜòõ)
  • cell-free protein synthesis
    ¹«¼¼Æ÷´Ü¹éÁúÇÕ¼º(Ùíá¬øàÓ±ÛÜòõùêà÷)
  • cellular retinol-binding protein
    ¼¼Æ÷(á¬øà) ·¹Æ¼³î°áÇÕ(Ì¿ùê) ´Ü¹éÁú(Ó±ÛÜòõ)
  • channel protein
    ä³Î ´Ü¹éÁú(Ó±ÛÜòõ)
  • chimeric protein
    Ű¸Þ¶ó ´Ü¹éÁú(Ó±ÛÜòõ)
  • cholesterol ester transfer protein
    ÄÝ·¹½ºÅ×·Ñ¿¡½ºÅÍ ÀüÀ̴ܹéÁú(ï®ì¹Ó±ÛÜòõ)
  • coat protein
    ¿ÜÇǴܹéÁú(èâù«Ó±ÛÜòõ)
  • competitive protein-binding technique
    °æÇÕÀû ´Ü¹éÁú °áÇÕ¼ú(ÌæùêîÜÓ±ÛÜòõÌ¿ùêâú)
  • complete protein
    ¿ÏÀü´Ü¹éÁú(èÇîïÓ±ÛÜòõ)
  • conjugated protein
    Á¢ÇմܹéÁú(ïÈùêÓ±ÛÜòõ)
  • contractile protein
    ¼öÃ༺ ´Ü¹éÁú(â¥õêàõÓ±ÛÜòõ)
  • copper protein
    µ¿´Ü¹éÁú(ÔÞÓ±ÛÜòõ)
  • core protein
    ÇٽɴܹéÁú(ú·ãýÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
MBP major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl...
RP radial pulse; radiopharmaceutical; rapid processing [of film]; Raynaud phenomenon; reactive protein;...
AP   1) Alkaline Phosphatase
    = ALP
  2) Amyloid Plasm...
ACP accessory conduction pathway; acid phosphatase; acyl carrier protein; American College of Pathologis...
EAP electric acupuncture; employee assistance program; epiallopregnanolone; Epstein-Barr associated prot...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
PTPase Protein tyrosine phosphatase
PTP1B Protein tyrosine phosphatase 1B
PTPalpha Protein tyrosine phosphatase alpha
RPTP alpha Receptor Protein-Tyrosine Phosphatase alpha
RPTP Receptor protein-tyrosine phosphatase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 8 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • protein hydrolysate
    ´Ü¹é ¼öÇØ¹°
    ´Ü¹éÁúÀ» »ê, ¾ËÄ®¸®, È¿¼Ò µîÀ¸·Î ºÐÇØÇÏ¿© »ý±â´Â ¾Æ¹Ì ³ë»êÀÇ È¥ÇÕ¹°·Î, À̰ÍÀ¸·Î ¾ò¾îÁö´Â Á¦Àç´Â ¾Æ¹Ì³ë»ê ¼ººÐÀ¸·Î º¼ ¶§, ¿ø·¡ÀÇ ¹°Áú°ú ¿µ¾çÇÐÀûÀ¸·Î µî°¡·Î¼­, º¸ÅëÀÇ ½ÄÀ̼º ´Ü¹éÀ» ¼·ÃëÇÏÁö ¸øÇϴ ȯÀÚ¿ë ¶Ç´Â Æ¯º°½ÄÀ¸·Î »ç¿ëµÈ´Ù.
  • protein polysaccharide
    ´Ü¹é ´Ù´ç·ù
  • protein-drug complex
    ´Ü¹é-¾à¹° º¹ÇÕü
  • protein-losing gastroenteropathy
    ´Ü¹é »ó½Ç¼º À§ÀåÁõ
  • serum amyloid protein A
    Ç÷û ¾Æ¹Ð·ÎÀ̵å ÇÁ·Îƾ A
  • serum protein
    Ç÷Àå ´Ü¹é
  • serum protein meter
    Ç÷û ´Ü¹é°è
    Ç÷û ´Ü¹é Á¤·®¿ëÀÇ ¼ÒÇü ±¼Àý°è.
  • silver protein mild
    ¾à·Â ÇÁ·ÎÅ×ÀÎ Àº
    Àº 19¡­23%¸¦ ÇÔÀ¯Çϰí, ´Ü¹éÁúÀÇ Á¸Àç ¶Ç´Â ´Ü¹é°úÀÇ °áÇÕ¿¡ ÀÇÇØ¼­ ÄÝ·ÎÀ̵åÈ­ÇÑ Á¦Á¦. ¾Ï°¥»ö ¶Ç´Â °ÅÀÇ Èæ»öÀÇ ºñ´Ã ¶Ç´Â °ú¸³À¸·Î¼­ Á÷Àå, ´«, Áú, ¿äµµ, ±Í, ÄÚ, ¹× ÀεΠµîÀÇ ¿©·¯ °¡Áö °¨¿°Áõ¿¡ ±¹¼Ò¿ë Ç×°¨¿°Á¦·Î »ç¿ëÇÑ´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
Gomori's non-specific acid phosphatase stain <technique> A method in which formalin-fixed frozen sections are incubated in a substrate containing sodium beta-glycerophosphate and lead nitrate at pH 5.0; the insoluble lead phosphate produced is treated with ammonium sulfide to give a black lead sulfide.
(05 Mar 2000)
Gomori's non-specific alkaline phosphatase stain <technique> A calcium-cobalt sulfide method using frozen sections or cold acetone-or formalin-fixed paraffin sections, plus sodium beta-glycerophosphate as a substrate at pH 9.0 to 9.5 with Mg++ as activator; calcium ions precipitate the liberated phosphate, cobalt salt replaces the calcium phosphate, and ammonium sulfide converts the product to a black cobalt sulfide.
(05 Mar 2000)
choline phosphatase <enzyme> An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyses transphosphatidylation reactions.
Chemical name: Phosphatidylcholine phosphatidohydrolase
Registry number: EC 3.1.4.4
(12 Dec 1998)
RNA-tyrosine phosphatase <enzyme> Hela cell enzyme which removes 5'-terminal protein from poliovirus RNA by breaking the tyrosine-phosphate bond between the above two entities
Registry number: EC 3.1.4.-
Synonym: uridylyl-(5'p-o)-tyrosine phosphodiesterase, y-pupnpde, tyrosine-RNA phosphatase, uridylylpolynucleotide-(5'p-o)-tyrosine phosphodiesterase
(26 Jun 1999)
chromatin 3'-phosphatase-5'-hydroxy kinase <enzyme> Hydrolyzes the 3'-phosphate end of a polynucleotide duplex followed by ATP-mediated phosphorylation of the 5'-oh end
Registry number: EC 3.1.3.-
Synonym: chromatin-phosphatase-hydroxykinase
(26 Jun 1999)
phenylalanine hydroxylase phosphatase <enzyme> Catalyses dephosphorylation of phosphorylated phenylalanine hydroxylase
Registry number: EC 3.1.3.-
Synonym: phe hydroxylase phosphatase
(26 Jun 1999)
phosphatase <enzyme> That hydrolyse phosphomonoesters. Acid phosphatases are specific for the single charged phosphate group and alkaline phosphatases for the double charged group. These specificities do not overlap.
The phosphatases comprise a very wide range of enzymes including broad and narrow specificity members. Phosphoprotein phosphatases specifically de phosphorylate a particular protein and are essential if phosphorylation is to be used as a reversible control system.
(31 Dec 1997)
phosphatase unit See: Bodansky unit, King unit.
(05 Mar 2000)
phosphatidate phosphatase <enzyme> A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyses the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate.
Chemical name: 3-sn-Phosphatidate phosphohydrolase
Registry number: EC 3.1.3.4
(12 Dec 1998)
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase <enzyme> Hydrolyzes the 5-position phosphate of ptdins(3,4,5)p3 forming phosphatidylinositol-3,4-bisphosphate; an isoenzyme forms a complex with the p85/p110 form of pi 3-kinase
Registry number: EC 3.1.3.-
Synonym: ptdins(3,4,5)p3 5-phosphatase, pi(3,4,5)p3 5-pase
(26 Jun 1999)
phosphatidylinositol-3-phosphatase <enzyme> Hydrolyzes phosphatidylinositol 3-phosphate in nih 3t3 cells; specific as it has little or no activity on the monoester phosphates of ptdins(4)p, ptdins(4,5)p2, or inositol 1,3-bisphosphate; does not require added metal ions for activity and is maximally active in the presence of edta; inhibited by ca(2+), mg(2+),zn(2+), and the phosphatase inhibitor vo(3-)4
Registry number: EC 3.1.3.64
Synonym: phosphatidylinositol 3-phosphatase
(26 Jun 1999)
phosphatidylinositol 4-phosphate phosphatase <enzyme> From human erythrocyte membranes
Registry number: EC 3.1.3.-
Synonym: ptdins-4p-phosphatase, phosphatidylinositol-4-phosphate monoesterase, ptdins4p monoesterase
(26 Jun 1999)
phosphocholine phosphatase <enzyme> Unlike alkaline phosphatase the hamster heart enzyme has a different pH optimum and heat sensitivity and is not inhibited by amino acids
Registry number: EC 3.1.3.-
(26 Jun 1999)
phosphofructokinase phosphatase <enzyme> May be an aspect of EC 3.1.3.16
Registry number: EC 3.1.3.-
Synonym: pfk-inactivating enzyme
(26 Jun 1999)
phospholamban phosphatase <enzyme> Purified from canine cardiac cytosol; dephosphorylates pholamban; stimulated by mg+2, mn+2 or ca+2
Registry number: EC 3.1.3.-
(26 Jun 1999)
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