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  • ¿µ¹®
    ÇѱÛ
  • gastric acid
    ˤȐ
  • gastric adenoma
    À§»ùÁ¾
  • gastric analysis
    À§¾×°Ë»ç
  • gastric anisakiasis
    À§°í·¡È¸ÃæÁõ
  • gastric artery
    À§µ¿¸Æ
  • gastric body
    À§¸öÅë
  • gastric canal
    À§¸öÅë°ü, À§µµ
  • gastric crisis
    À§±ÞÅëÁõ
  • gastric dilatation
    À§È®Àå
  • gastric dyspepsia
    À§(¼º)¼ÒÈ­ºÒ·®
  • gastric emptying time
    À§¹èÃâ½Ã°£
  • gastric feeding
    À§¿µ¾ç, À§±Þ½Ä
  • gastric filling
    À§Ã游
  • gastric flatulence
    À§³»°ø±âÂü, À§°íâ
  • gastric fundus
    À§¹Ù´Ú
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  • ¿µ¹®
    ÇѱÛ
  • gastric crisis
    À§±ÞÅëÁõ
  • delayed gastric emptying
    Áö¿¬À§¹èÃâ, Áö¿¬À§ºñ¿ì±â
  • gastric dilatation
    À§È®Àå
  • gastric dyspepsia
    À§¼ÒÈ­ºÒ·®
  • gastric filling
    À§Ã游
  • gastric flatulence
    À§°¡½ºÆØ¸¸À½, À§°íâ
  • gastric replacement fluid
    À§´ëÄ¡¾×, À§º¸¾×
  • gastric scarlet fever
    À§¼ºÈ«¿­
  • gastric
    ˤ-
  • gastric gland
    ˤȝ
  • gastric hyperacidity
    (¢¡hyperchlorhydria) °ú´Ù¿°»ê(Áõ)
  • gastric hypersecretion
    (¢¡hyperchlorhydria) °ú´Ù¿°»ê(Áõ)
  • gastric motility
    À§¿îµ¿
  • gastric notch
    (¢¡angular notch) ¸ðÆÐÀÓ
  • gastric pit
    À§¿À¸ñ
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  • ¿µ¹®
    ÇѱÛ
  • Gastric glands
    À§¼±(êÖàÍ)
  • Gastric mucosa
    À§Á¡¸·(êÖïÄØ¯)
  • Gastric reflux
    À§¹Ý»ç(êÖÚãÞÒ)
  • Gastric slow wave
    À§¼­ÆÄ(êÖßï÷î)
  • Gastric tone
    À§Àå±äÀåµµ(êÖíóÑÌíåÓø)
  • acute gastric dilatation
    ±Þ¼º À§È®Àå(Áõ) (¡­êÖüªíåñø).
  • adenoma,gastric polypoid
    À§ Æú¸³¸ð¾ç(êÓ¡­Ù¼åÆ)
  • anterior gastric branches
    ¾ÕÀ§°¡Áö
  • gastric
    ˤ˂.
  • gastric
    À§(ÀÇ)(êÖ)
  • gastric abscess
    À§³ó¾ç.
  • gastric achylia
    À§¾×°áÇÌ(Áõ).
  • gastric acid
    À§»ê(ß«)
  • gastric acid secretion
    À§(êÖ)(¾×(äû))»êºÐºñ(ß«ÝÂÝô).
  • gastric acid secretory studies
    À§»êºÐºñ °Ë»ç.
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  • ¿µ¹®
    ÇѱÛ
  • inhibitory autacoid
    ¾ïÁ¦¿À¿ÀŸÄÚÀ̵å.
  • inhibitory concentration, minimum (MIC)
    ¾ïÁ¦ÃÖ¼Ò³óµµ
  • inhibitory effect
    ¾ïÁ¦È¿°ú.
  • inhibitory effect
    ¾ïÁ¦È¿°ú(åäð¤ Íý).
  • inhibitory enzyme
    ÀúÇØÈ¿¼Ò.
  • inhibitory hormone
    ¾ïÁ¦(åäð¤)È£¸£¸ó.
  • inhibitory junctional potential
    ¾ïÁ¦¼º Á¢ÇÕºÎÀü¾Ð(ïÈùêݬï³äâ).
  • inhibitory nerve
    ¾ïÁ¦½Å°æ.
  • inhibitory nerve
    ¾ïÁ¦½Å°æ(åäð¤ãêÌè).
  • inhibitory postsynaptic potential
    ¾ïÁ¦¼º ½Ã³³½ºÈÄÀü¾Ð.
  • inhibitory postsynaptic potential
    ¾ïÁ¦¼º ½Ã³³½ºÈÄ Àü¾Ð
  • inhibitory postsynaptic potential = IPSP
    ¾ïÁ¦¼º ½Ã³³½ºÈÄÀü¾Ð.
  • inhibitory synapse
    ¾ïÁ¦¼º ½Ã³³½º.
  • inhibitory synapse
    ¾ïÁ¦¼º(åäð¤àõ) ½Ã³³½º.
  • inhibitory transmitter
    ¾ïÁ¦¼º Àü´Þ¹°Áú.
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PIF   1) Proliferation Inhibitory Factor
  2) Prolactin release Inhibiting Factor...
SRIF Somatotropin Release-Inhibitory Factor
  = Somatostatin
CIF cloning inhibitory factor
CIS carcinoma in situ; catheter-induced spasm; central inhibitory state; Chemical Information Service; c...
CLIF cloning inhibitory factor; Crithidia luciliae immunofluorescence
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
G E)-gastric
E.G.C. Early Gastric Cancer
EGC Early gastric carcinoma
GU Gastric
GBP Gastric Bypass
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • inhibitory hormone
    ¾ïÁ¦ È£¸£¸ó
    Ç¥Àû ±â°ü¿¡ ´ëÇÏ¿© ¾ïÁ¦ÀûÀ¸·Î ÀÛ¿ëÇϴ ȣ¸£¸ó.
  • inhibitory input
    ¿ªÁ¦¼º ÀÔ·Â
  • inhibitory interneuron
    ¾ïÁ¦ °³Àç ´º¿ì·±
  • inhibitory output cell
    ¾ïÁ¦ Ãâ·Â ¼¼Æ÷
  • inhibitory postsynaptic potential
    ¾ïÁ¦¼º ½Ã³³½ºÈÄ Àü¾Ð
    ¾ïÁ¦¼º ±¸½É·Î¿¡ ÀÏÁ¦È÷ Ãæµ¿ÀÌ °¡ÇØÁú ¶§ ½Ã³À½º ÈÄ ´º·Ð¿¡ ¹ßÇàÇÏ´Â ¸·ÀüÀ§ÀÇ Àϰú¼º °úºÐ±ØÀ̸ç, ÀÌ ¶§¹®¿¡ ½Å°æ ´ÜÀ§ÀÇ ¹ÝÀÀ¼ºÀÌ °¨¾àµÈ´Ù.
  • inhibitory substantia gelatinosa cell
    ¾ïÁ¦¼º ±³¾çÁú ¼¼Æ÷
  • inhibitory synapse
    ¾ïÁ¦¼º ½Ã³³½º
  • light touch inhibitory
    ºÒºû ÀÚ±Ø ¾ïÁ¦
  • macrophage migration inhibitory factor
    ´ë½Ä ¼¼Æ÷ À¯ÁÖ ÀúÁö ÀÎÀÚ, °Å½Ä ¼¼Æ÷ À¯ÁÖ ¾ïÁ¦ ÀÎÀÚ
  • migration inhibitory factor test
    À¯ÁÖ ÀúÁö ÀÎÀÚ ½ÃÇè
    ƯÀÌ Ç׿ø¿¡ ¹ÝÀÀÇÏ¿© ¸²ÇÁ±¸°¡ MIF¸¦ »ý¼ºÇÏ´Â µ¥ ´ëÇÑ »ýüÀÇ ½ÃÇè¹ýÀ¸·Î ¼¼Æ÷ ¸Å°³ ¸é¿ªÀ» Æò°¡ÇÏ´Â µ¥ »ç¿ëÇÑ´Ù. ÀϺΠ¸é¿ª °áÇÌ Áúº´, Áï DiGeorge ÁõÈıº, Wiskott-Aldrich ÁõÈıº, Hodgkin º´¿¡¼­´Â MIF°¡ »ý¼ºµÇÁö ¾Ê´Â´Ù.
  • minimum inhibitory dose
    ÃÖ¼Ò ¾ïÁ¦·®
  • peripheral inhibitory field
    ¸»ÃÊ ¾ïÁ¦¾ß
  • presynaptic inhibitory action
    ½Ã³³½ºÀü ¾ïÁ¦ ÀÛ¿ë
  • virus inhibitory factor
    ¹ÙÀÌ·¯½º ¾ïÁ¦ ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
peptide antibiotic lactonase <enzyme> Peptide lactone and water gives linear peptide
Registry number: EC 3.1.1.-
(26 Jun 1999)
peptide bond The amide linkage between the carboxyl group of one amino acid and the amino group of another. The linkage does not allow free rotation and can occur in cis or trans configuration, the latter the most common in natural peptides, except for links to the amino group of proline, which are always cis.
(18 Nov 1997)
peptide chain elongation The process whereby an amino acid is joined through a substituted amide linkage to a chain of peptides.
(12 Dec 1998)
peptide chain initiation The process whereby the formation of a peptide chain is started. This process requires (1) the 30s subunit, (2) the mRNA coding for the polypeptide to be made, (3) met-trnai, (4) initiation factors, and (5) GTP.
(12 Dec 1998)
peptide chain termination The process whereby the last amino acid is added to a polypeptide. This termination is signaled by one of three termination triplets in the mRNA, immediately following the last amino acid codon.
(12 Dec 1998)
peptide deformylase <enzyme> Fms is a zinc-containing protein showing homologies with zinc aminopeptidases; its enzyme function resembles that of an aminopeptidase; has been sequenced; mol mass 19,207 da
Registry number: EC 3.4.11.-
Synonym: fms protein, fms gene product
(26 Jun 1999)
peptide elongation factors Protein factors uniquely required during the elongation phase of protein synthesis.
(12 Dec 1998)
peptide elongation factor tu A protein found in bacteria and eukaryotic cells which delivers aminoacyl-trna's to the a site of the ribosome. The aminoacyl-trna is first bound to a complex of elongation factor tu containing a molecule of bound GTP. The resulting complex is then bound to the 70s initiation complex. Simultaneously the GTP is hydrolyzed and a tu-GDP complex is released from the 70s ribosome. The tu-GTP complex is regenerated from the tu-GDP complex by the ts elongation factor and GTP.
(12 Dec 1998)
peptide hormone inactivating endopeptidase <enzyme> From xenopus laevis; cleaves at xaa-phe, xaa-leu or xaa-ile bonds where xaa = ser, phe, tyr, his or gly in peptide hormones
Registry number: EC 3.4.24.-
Synonym: phie, xenopus
(26 Jun 1999)
peptide hydrolases <enzyme> Registry number: EC 3.4
(12 Dec 1998)
peptide initiation factors Protein factors uniquely required during the initiation phase of protein synthesis.
(12 Dec 1998)
peptide library A collection of cloned free peptides, frequently consisting of all possible combinations of amino acids making up an n-amino acid peptide.
(12 Dec 1998)
peptide map Proteases will produce fragments of a characteristic size from a protein and this can be used as a test for the identity or otherwise of two similar sized proteins. It is possible to produce a peptide fragment map from a single gel band.
(18 Nov 1997)
peptide mapping Two-dimensional separation and analysis of peptides.
(12 Dec 1998)
peptide N-alpha acetyltransferase <enzyme> Pituitary enzyme; acetylates peptide hormones including acth; also found in saccharomyces cerevisiae
Registry number: EC 2.3.1.88
Synonym: peptide acetyltransferase, acth acetyltransferase, beta-endorphin acetyltransferase, alpha-msh acetyltransferase
(26 Jun 1999)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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