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  • ¿µ¹®
    ÇѱÛ
  • phosphorylase
    ÀλêÈ­È¿¼Ò
  • phosphorylase kinase
    Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦Å°³ª¾ÆÁ¦
  • acid phosphatase
    »ê¼ºÀλêºÐÇØÈ¿¼Ò
  • alkaline phosphatase
    ¾ËÄ®¸®ÀλêºÐÇØÈ¿¼Ò
  • glucose-6-phosphatase
    Æ÷µµ´çÀ°ÀλêÈ­È¿¼Ò, ±Û·çÄÚ¿À½º-6-Æ÷½ºÆÄŸ¾ÆÁ¦
  • phosphatase
    ÀλêºÐÇØÈ¿¼Ò
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  • ¿µ¹®
    ÇѱÛ
  • phosphorylase
    ÀλêÈ­È¿¼Ò
  • phosphatase
    ÀλêºÐÇØÈ¿¼Ò
  • alkaline phosphatase
    ¾ËÄ®¸®ÀλêºÐÇØÈ¿¼Ò
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  • ¿µ¹®
    ÇѱÛ
  • phosphorylase
    ÀλêÈ­È¿¼Ò
  • acid phosphatase
    »ê¼ºÀλêºÐÇØÈ¿¼Ò
  • glucose-6-phosphatase
    Æ÷µµ´çÀ°ÀλêÈ­È¿¼Ò, ±Û·çÄÚ¿À½º-6-Æ÷½ºÆÄŸ¾ÆÁ¦
  • phosphatase
    ÀλêºÐÇØÈ¿¼Ò
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  • ¿µ¹®
    ÇѱÛ
  • glycogen phosphorylase
    ±Û¸®ÄÚ°ÕÆ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • inosine phosphorylase deficiency
    À̳ë½ÅÆ÷½ºÆ÷¸±¶óÁ¦°áÇÌ(Áõ)
  • phosphorylase
    Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • phosphorylase =PR
    Æ÷½ºÆ÷¸±·¹À̽º.
  • phosphorylase kinase
    Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦Å°³ª¾ÆÁ¦
  • purine nucleoside phosphorylase
    Ç»¸° ´©Å¬·¹¿À½Ãµå Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • 2,3-diphosphoglycerate phosphatase
    2,3-ÀÌÀλê±Û¸®¼¼¸°»êÀλêÈ¿¼Ò
  • Glucose phosphatase
    Àλê(×òß«)±Û·çÄÚ¿À½º
  • acid phosphatase
    »êÀλêÈ¿¼Ò
  • acid phosphatase
    »ê¼ºÆ÷½ºÆÄŸÁ¦
  • acid phosphatase
    »ê¼ºÆ÷½ºÆÄÅ×À̽ºÁ¦.
  • acid phosphatase
    »ê¼º Æ÷½ºÆÄÅ×À̽º(ß«àõ¡­)
  • acid phosphatase
    »ê¼ºÀλêÈ¿¼î
  • acid phosphatase assay
    »ê¼ºÆ÷½ºÆÄŸÁ¦ ÃøÁ¤
  • glucose 3 phosphatase =G-3-P
    ±Û·çÄÚ¿À½º-3-Æ÷½ºÆÄŸÁ¦.
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  • ¿µ¹®
    ÇѱÛ
  • glycogen phosphorylase
    ±Û¸®ÄÚ°ÕÆ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • inosine phosphorylase deficiency
    À̳ë½ÅÆ÷½ºÆ÷¸±¶óÁ¦°áÇÌ(Áõ)
  • muscle phosphorylase
    ±ÙÆ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • phosphorylase
    Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • phosphorylase =PR
    Æ÷½ºÆ÷¸±·¹À̽º.
  • phosphorylase kinase
    Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦Å°³ª¾ÆÁ¦
  • purine nucleoside phosphorylase
    Ç»¸° ´©Å¬·¹¿À½Ãµå Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦
  • acid phosphatase
    »êÀλêÈ¿¼Ò
  • acid phosphatase
    »ê¼ºÀλêÈ¿¼î
  • acid phosphatase
    »ê¼ºÆ÷½ºÆÄÅ×À̽ºÁ¦.
  • acid phosphatase
    »ê¼º Æ÷½ºÆÄÅ×À̽º(ß«àõ¡­)
  • acid phosphatase
    »ê¼ºÆ÷½ºÆÄŸÁ¦
  • acid phosphatase assay
    »ê¼ºÆ÷½ºÆÄŸÁ¦ ÃøÁ¤
  • alkaline phosphatase
    ¾ËÄ®¸®¼º Æ÷½ºÆÄÅ×À̽º.
  • alkaline phosphatase
    ¾ËÄ«¸® ÀλêºÐÇØÈ¿¼Ò(¡­×òß«ÝÂú°ý£áÈ)
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  • ¿µ¹®
    ÇѱÛ
  • phosphorylase phosphatase
    Æ÷½ºÆ÷¸±·¹À̽ºÆ÷½ºÆÄÅ×À̽º
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  • ¿µ¹®
    ÇѱÛ
  • acid phosphatase
    »ê¼º(ß«àõ) Æ÷½ºÆÄÅ×À̽º
  • alkaline phosphatase
    ¾ËÄ®¸®¼º Æ÷½ºÆÄÅ×À̽º
  • glucose-6-phosphatase
    ±Û·çÄÚ½º-6-Æ÷½ºÆÄÅ×À̽º
  • phosphatase
    Æ÷½ºÆÄÅ×À̽º
  • phosphoprotein phosphatase
    Àλê´Ü¹éÁú(×ò߫ӱÛÜòõ) Æ÷½ºÆÄÅ×À̽º
  • glycogen phosphorylase
    ±Û¶óÀÌÄÚÀü Æ÷½ºÆ÷¸±·¹À̽º
  • phosphorylase
    Æ÷½ºÆ÷¸±·¹À̽º
  • phosphorylase kinase
    Æ÷½ºÆ÷¸±·¹À̽ºÄ«À̳×À̽º
  • polynucleotide phosphorylase
    Æú¸®´©Å¬·¹¿ÀŸÀÌµå Æ÷½ºÆ÷¸±·¹À̽º
  • polyribonucleotide phosphorylase
    Æú¸®¶óÀ̺¸´©Å¬·¹¿ÀŸÀÌµå Æ÷½ºÆ÷¸±·¹À̽º
  • polysaccharide phosphorylase
    ´Ù´çÁú(ÒýÓØòõ) Æ÷½ºÆ÷¸±·¹À̽º
  • starch phosphorylase
    ³ì¸» Æ÷½ºÆ÷¸±·¹À̽º
  • synthase-phosphorylase kinase
    ½ÅÅ×À̽º-Æ÷½ºÆ÷¸±·¹À̽º Ä«À̳×À̽º
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • phosphatase
    Æ÷½ºÆÄŸÁ¦, ÀλêÈ¿¼Ò
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
AP accessory pathway; accounts payable; acid phosphatase; acinar parenchyma; action potential; active p...
APAAP alkaline phosphatase-antialkaline phosphatase [labeling]
NAP nasion, point A, pogonion [convexity or concavity of the facial profile]; nerve action potential; ne...
PAP pancreatitis-associated protein; Papanicolaou [test]; papaverine; passive-aggressive personality; pa...
SAP sensory action potential; serum acid phosphatase; serum alkaline phosphatase; serum amyloid P; situs...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
APAAP Alkaline Phosphatase anti-Alkaline Phosphatase
GP Glycogen Phosphorylase
MTAP Methylthioadenosine phosphorylase
NP Nucleoside phosphorylase
PHK Phosphorylase kinase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 6 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • nucleoside phosphorylase
    ´ºÅ¬·¹¿À½Ãµå Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦
    ´ºÅ¬·¹¿À½Ãµå¸¦ °¡ÀλêºÐÇØÇÏ¿© Ç»¸°, ÇǸ®¹Ìµò ¿°±â¿Í ÆæÅä¿À½º ÀλêÀ» »ý¼ºÇÏ´Â ¹ÝÀÀ¿¡ °ü¿©ÇÏ´Â È¿¼Ò. ±âÁú ƯÀ̼ºÀÌ ´Ù¸¥ °ÍÀÌ ¸î °¡Áö ¾Ë·ÁÁ® ÀÖ´Ù. ¿¹¸¦ µé¸é, Ç»¸° ´ºÅ¬·¹¿À½Ãµå Æ÷½ºÆ÷¸±¶ó¾ÆÁ¦´Â ±¸¾Æ³ë½Å, µð¿Á½Ã±¸¾Æ³ë½Å, À̳ë½Å, µð¿Á½ÃÀ̳ë½Å¿¡ ÀÛ¿ëÇϸç, Áö¶ó, Æó, °£, ½É±Ù, ÀûÇ÷±¸, È¿¸ð¿¡, ¼Ò·®Àº ¼ÒÀå, Ç÷¾×¿¡ ÀÖ´Ù. ±×¹Û¿¡ ÇǸ®¹Ìµò ´ºÅ¬·¹¿À½Ãµå Æ÷½ºÆ÷ ¸±¶ó¾ÆÁ¦·Î¼­ ¿ì¸®µò, Ƽ¹Ìµò¿¡ °¢°¢ ƯÀÌÀûÀÎ È¿¼Ò°¡ ¾Ë·ÁÁ® ÀÖ´Ù. ÁÖ·Î ´ºÅ¬·¹¿À½ÃµåÀÇ ºÐÇØ, ¶Ç´Â ´Ù¸¥ Á¾·ùÀÇ ´ºÅ¬·¹¿À½Ãµå »ý¼ºÀ» À§ÇÑ ¸®º¸¿À½ºÀλêÀ» °ø±ÞÇÏ´Â ¿ªÇÒÀ» ÇÑ´Ù.
  • acid phosphatase assay
    »ê¼º Æ÷½ºÆÄŸÁ¦ ÃøÁ¤
  • alkaline phosphatase antialkaline phophatase method
    ¾ËÄ®¸®¼º Æ÷½ºÆÄŸÁ¦ Ç×¾ËÄ®¸®¼º Æ÷½ºÆÄŸÁ¦¹ý
  • phosphatase
    Æ÷½ºÆÄŸÁ¦, Àλê È¿¼Ò
    ÀÎ»ê ¿¡½ºÅͷκÎÅÍ ¹«±â Àλ꿰À» À¯¸®½Ã۴µ¥ Ã˸ÅÀÛ¿ëÀ» ÇÏ´Â °¡¼öºÐÇØ È¿¼ÒÀÇ Ãʾư­ÀÇ ÃÑĪ.
  • serum alkaline phosphatase
    Ç÷û ¾ËÄ«¸® Æ÷½ºÆÄŸ¾ÆÁ¦
  • total acid phosphatase
    Ãѻ꼺 ÀÎ»ê ºÐÇØ È¿¼Ò, Ãѻ꼺 Æ÷½ºÆÄŸÁ¦
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
phosphorylase phosphatase <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form.
Chemical name: (Phosphorylase a) phosphohydrolase
Registry number: EC 3.1.3.17
(12 Dec 1998)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
phosphorylase kinase phosphatase <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16
Registry number: EC 3.1.3.-
(26 Jun 1999)
alpha,alpha-trehalose phosphorylase <enzyme> Chemical name: alpha-d-glucopyranosyl-alpha-d-glucopyranose orthophosphate glucosyltransferase
Registry number: EC 2.4.1.64
Synonym: trehalose phosphorylase
(26 Jun 1999)
alpha-glucan phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
(21 Jun 2000)
maltodextrin phosphorylase <enzyme> From E coli
Registry number: EC 2.4.1.-
Synonym: e350a
(26 Jun 1999)
GDPmannose phosphorylase <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate.
Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases
Registry number: EC 2.7.7.13
Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein
(26 Jun 1999)
cellodextrin phosphorylase <enzyme> Reverse reaction is used to synthesise cellodextrins
Registry number: EC 2.4.1.49
(26 Jun 1999)
glycogen phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
(21 Jun 2000)
phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
(21 Jun 2000)
phosphorylase a <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate.
Registry number: EC 2.4.1.-
(12 Dec 1998)
phosphorylase b <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP.
Registry number: EC 2.4.1.-
(12 Dec 1998)
phosphorylase kinase <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle.
(18 Nov 1997)
phosphorylase-rupturing enzyme <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form.
Chemical name: (Phosphorylase a) phosphohydrolase
Registry number: EC 3.1.3.17
(12 Dec 1998)
muscle phosphorylase deficiency Type V glycogen storage disease, affecting muscle, caused by deficiency of muscle phosphorylase.
(05 Mar 2000)
polynucleotide phosphorylase <enzyme> An enzyme of the transferase class that catalyses the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, idp, GDP, udp, and cdp can act as donors in the latter case.
Chemical name: Polyribonucleotide:orthophosphate nucleotidyltransferase
Registry number: EC 2.7.7.8
(12 Dec 1998)
xanthosine phosphorylase <enzyme> From E coli k-12; mw 18kda; inactivated by p-chloromercuriphenylsulfonic acid
Registry number: EC 2.4.2.-
Synonym: inosine-guanosine phosphorylase
(26 Jun 1999)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Phosphorylase Phosphatase - »õâ An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.
    Synonyms : Glycogen Phosphorylase Phosphatase, Phosphatase, Glycogen Phosphorylase, Phosphatase, Phosphorylase, Phosphorylase Phosphatase, Glycogen
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