¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"lysine carboxypeptidase"¿¡ ´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 : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼµåºÐÇØÈ¿¼Ò
  • lysine
    ¸®½Å
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼµåºÐÇØÈ¿¼Ò
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼµåºÐÇØÈ¿¼Ò
  • lysine
    ¶óÀ̽Å
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Lysine
    ¿ëÇØ¼Ò(éÁú°áÈ)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 6 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼ´ÙÁ¦
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼµ¥À̽º.
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼ´ÙÁ¦, Ä«¸£º¹½ÃÆéƼµ¥À̽º
  • lysine
  • lysine-iron agar
    ¸®Áø-ö ÇÑõ
  • xylose-lysine-deoxycholate medium
    ½Ç·Î½º-¸®½Å-µ¥¿Á½ÃÄÝ·¹ÀÌÆ®¹èÁö
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxypeptidase
    Ä«¸£º¹½ÃÆéƼµ¥À̽º
  • lysine
    ¶óÀ̽Å
  • lysine intolerance
    ¶óÀ̽ŰźÎÁõ(ËÞÜúñø)
  • lysine vasopressin
    ¶óÀ̽Š¹Ù¼ÒÇÁ·¹½Å
  • lysine vasotocin
    ¶óÀ̽Š¹Ù¼ÒÅä½Å
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
ACE Angiotensin Converting Enzyme
  = Kininase II
  = Dipeptidyl Carboxypepti...
CPA Canadian Physiotherapy Association; Canadian Psychiatric Association; carboxypeptidase A; cardiopulm...
CPB carboxypeptidase B; cardiopulmonary bypass; cetylpyridinium bromide; competitive protein binding
SCPN serum carboxypeptidase N
PPL Penicilloyl Poly-Lysine
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
CPase Carboxypeptidase
CP-A Carboxypeptidase A
CPB Carboxypeptidase B
CPD Carboxypeptidase D
CPE Carboxypeptidase E
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • lysine
    ¸®½Å
    1. ´Ü¹éÀ» °¡¼öºÐÇØÇÒ ¶§ »ý¼ºµÇ´Â ¾Æ¹Ì³ë»ê. 2. ¿°±â¼º ¥á-¾Æ¹Ì³ë»êÀÇ Çϳª. È­ÇнÄÀº HN
  • C3a : C3ÀÇ ¥á¼âÀÇ N ¸»´ÜÀÌ C3 Àüȯ È¿¼Ò³ª Æ®¸³½Å µî¿¡ ÀÇÇÏ¿© Àý´ÜµÇ¾î »ý±ä ÀúºÐÀÚÀÇ ¿°±â¼º Æú¸® ÆéŸÀ̵å. AnaphylatoxinÀ¸·Î¼­ÀÇ È°¼ºÀÌ ÀÖ°í ÀÌ È°¼ºÀº C3aÀÇ C ¸»´Ü ¾Æ¸£±â´ÑÀ» Á¦°ÅÇÏ´Â Ç÷û ¼ÓÀÇ carboxypeptidase B¶ó°í ÇÏ´Â anaphylatoxin ºÒ Ȱ¼ºÈ­ ÀÎÀÚ¿¡ ÀÇ
    C3b ºÒ Ȱ¼ºÈ­ ÀÎÀÚ
    Conglutinogen Ȱ¼ºÈ­ ÀÎÀÚ¶ó°íµµ ºÒ¸®¿ì°í ÀÖ¾úÁö¸¸ ÇöÀç´Â I ÀÎÀÚ·Î ºÒ¸®¿ì°Ô µÇ¾î ÀÖ´Ù. C3¿¡´Â ÀÛ¿ëÇÏÁö ¾ÊÁö¸¸ C3 Àüȯ È¿¼Ò¿¡ ÀÇÇÏ¿© »ý±ä C3b¿¡ H ÀÎÀÚ¿Í ÇÔ²² ÀÛ¿ëÇÏ¿© C3b¸¦ C3c¿Í C3b·Î ºÐÇØÇϰí C3b¿¡ ÀÖ´Â ¿ëÇ÷ Ȱ¼º, ¸é¿ª ºÎÂø ¹ÝÀÀ, ¸é¿ª Ž½Ä µîÀÇ È°¼ºÀ» ÀúÇØÇϵµ·Ï ÀÛ¿ëÇÑ´Ù.
  • carboxypeptidase
    Ä«¸£º¹½Ã ÆéƼ´ÙÁ¦
    À¯¸® Ä«¸£º¹½Ç±â¸¦ °¡Áø ¸»´Ü ¾Æ¹Ì³ë»êÀÇ ÆéŸÀÌµå °áÇÕÀ» Âɰ³´Â µÎ °³ÀÇ °¡¼öºÐÇØ È¿¼Ò Áß Çϳª.
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
lysine carboxypeptidase <enzyme> A serine carboxypeptidase that removes c-terminal amino acids, preferentially lysine, from peptides and proteins. It inactivates bradykinin by this action.
Registry number: EC 3.4.17.3
(12 Dec 1998)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
acetyl-CoA - lysine N6-acetyltransferase <enzyme> First step in catabolism of lysine by saccharomyces cerevisiae
Registry number: EC 2.3.1.-
Synonym: accoa lysine acetyltransferase, lysine n-6-acetyltransferase, lyc1 gene product
(26 Jun 1999)
acid carboxypeptidase <enzyme> Carboxypeptidase z (scpz gene product) isolated from absidia zychae
Registry number: EC 3.4.16.1
Synonym: carboxypeptidase w, carboxypeptidase yscy, carboxypeptidase cpd-s3, ybr1015 gene product, carboxypeptidase z, scpz gene product
(26 Jun 1999)
alanine carboxypeptidase <enzyme> Not for d-ala linkage in peptidoglycan see EC 3.4.17.8
Registry number: EC 3.4.17.6
(26 Jun 1999)
angiotensin-related carboxypeptidase <enzyme> Rat and bovine brain synaptosomal enzyme can hydrolyze angiotensin I to des-leu angiotensin I, but no further
Registry number: EC 3.4.-
Synonym: angiotensin-specific carboxypeptidase
(26 Jun 1999)
carboxypeptidase <enzyme> Enzymes (particularly of pancreas) that remove the C terminal amino acid from a protein or peptide. Carboxypeptidase A, will remove any amino acid, carboxypeptidase B is specific for terminal lysine or arginine.
(18 Nov 1997)
carboxypeptidase A A hydrolase that releases C-terminal amino acids, with the exception of C-terminal arginyl, lysyl, and prolyl residues. A zinc-containing exopeptidase.
(05 Mar 2000)
carboxypeptidase B A hydrolase that releases C-terminal lysyl or arginyl residues preferentially. A zinc-containing exopeptidase.
Synonym: protaminase.
(05 Mar 2000)
carboxypeptidase C See: serine carboxypeptidase.
(05 Mar 2000)
carboxypeptidase G N-Pteroyl-l-glutamate hydrolase;an enzyme cleaving l-glutamyl residues from pteridine oligoglutamates; used in certain antitumour treatments.
Synonym: carboxypeptidase G, conjugase, gamma-glutamate (glutamate gamma-) carboxypeptidase.
(05 Mar 2000)
gamma-glutamate (glutamate gamma-) carboxypeptidase N-Pteroyl-l-glutamate hydrolase;an enzyme cleaving l-glutamyl residues from pteridine oligoglutamates; used in certain antitumour treatments.
Synonym: carboxypeptidase G, conjugase, gamma-glutamate (glutamate gamma-) carboxypeptidase.
(05 Mar 2000)
vitellogenic carboxypeptidase <enzyme> Serine carboxypeptidase synthesised in mosquito fat bodies and taken up into oocytes
Registry number: EC 3.4.16.-
(26 Jun 1999)
muramoylpentapeptide carboxypeptidase <enzyme> Enzyme produced by streptomyces strain r61 which catalyses the peptide cross-linking of nascent cell-wall peptidoglycan.
Registry number: EC 3.4.17.8
(12 Dec 1998)
cysteine carboxypeptidase <enzyme> An enzyme which removes the last peptide bond on a protein (the one at the carboxyl end). Its active site contains the sulphur part of the amino acid cysteine.
(09 Oct 1997)
procollagen-lysine, 2-oxoglutarate 5-dioxygenase <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of peptidyllysine, usually in protocollagen, to peptidylhydroxylysine. The enzyme utilises molecular oxygen with concomitant oxidative decarboxylation of the cosubstrate 2-oxoglutarate to succinate.
Chemical name: Procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Registry number: EC 1.14.11.4
(12 Dec 1998)
protein-lysine 6-oxidase <enzyme> An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide.
Chemical name: Protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
Registry number: EC 1.4.3.13
(12 Dec 1998)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Lysine Carboxypeptidase - »õâ A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.
    Synonyms : Anaphylatoxin Inactivator, Bradykininase, Carboxypeptidase, Lysine, Inactivator, Anaphylatoxin
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
lysine carboxypeptidase [EC 3.4.17.3] an enzyme of the hydrolase class that catalyzes the removal of C-terminal basic amino acids from peptides, preferentially removing lysine residues but also removing arginine residues from kinins, inactivating them. The enzyme is found in plasma. Called also arginine carboxypeptidase and kininase I.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • lysine
    ¸®Áø(¾Æ¹Ì³ë»êÀÇ ÀÏÁ¾)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á