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"antigen binding capacity"¿¡ ´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
  • antigen receptor
    Ç׿ø¼ö¿ëü
  • antigen recognition
    Ç׿øÀνÄ
  • antigen-antibody complex
    Ç׿øÇ×üº¹ÇÕü
  • antigen-antibody interaction
    Ç׿øÇ×ü»óÈ£ÀÛ¿ë
  • antigen-antibody reaction
    Ç׿øÇ×ü¹ÝÀÀ
  • antigen-combining site
    Ç׿ø°áÇÕºÎÀ§
  • antigen-presenting cell
    Ç׿øÁ¦½Ã¼¼Æ÷
  • antigen-reactive cell
    Ç׿ø¹ÝÀÀ¼¼Æ÷
  • antigen-recognition site
    Ç׿øÀÎÁöºÎÀ§
  • antigen-recognizing cell
    Ç׿øÀÎÁö¼¼Æ÷
  • avidin-antigen conjugate
    ¾ÆºñµòÇ׿øÁ¢ÇÕü
  • capsid antigen
    ĸ½ÃµåÇ׿ø
  • capsular antigen
    ÇǸ·Ç׿ø
  • common antigen
    °øÅëÇ׿ø
  • complete antigen
    ¿ÏÀüÇ׿ø
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  • ¿µ¹®
    ÇѱÛ
  • antigen mimicry
    Ç׿øÀ¯»ç¼º
  • antigen modification
    Ç׿øº¯È­, Ç׿ø¼ö½Ä
  • antigen presentation
    Ç׿øÀü´Þ
  • antigen receptor
    Ç׿ø¼ö¿ëü
  • antigen recognition
    Ç׿øÀÎÁö
  • antigen analysis
    Ç׿øºÐ¼®
  • antigen capture assay
    Ç׿øÆ÷È¹ÃøÁ¤
  • antigen diffusion constant
    Ç׿øÈ®»ê»ó¼ö
  • antigen excess zone
    Ç׿ø°úÀ×±¸¿ª
  • antigen-antibody complex
    Ç׿øÇ×üº¹ÇÕü
  • antigen-antibody interaction
    Ç׿øÇ×ü¹ÝÀÀ
  • antigen-antibody reaction
    Ç׿øÇ×ü¹ÝÀÀ
  • antigen-combining site
    Ç׿ø°áÇÕºÎÀ§
  • antigen-presenting cell
    Ç׿øÀü´Þ¼¼Æ÷
  • antigen-reactive cell
    Ç׿ø¹ÝÀÀ¼¼Æ÷
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  • ¿µ¹®
    ÇѱÛ
  • EBV capsid antigen (VCA)
    EB¹ÙÀÌ·¯½º ĸ½ÃµåÇ׿ø
  • EBV membrane antigen
    EB¹ÙÀÌ·¯½º ¸·Ç׿ø
  • EBV membrane antigen (MA)
    EB¹ÙÀÌ·¯½º ¸·Ç׿ø
  • Forssman antigen
    Æ÷½º¸¸Ç׿ø
  • Fy antigen/antibody
    Fy Ç׿ø/Ç×ü
  • Gag => group specifiic antigen/core
    ±×·ì<±º>ƯÀ̼º Ç׿ø/ÄÚ¾î
  • Gag antigen in HIV infection
    HIV °¨¿°ÀÇ gag Ç׿ø
  • Gag antigen:
    gag Ç׿ø
  • H antigen
    H Ç׿ø
  • H antigen
    HÇ׿ø, Æí¸ðÇ׿ø
  • H-Y histocompatibility antigen
    H-Y Á¶Á÷ÀûÇÕ¼º Ç׿ø
  • HBc Ag => hepatitis B core antigen
    B Çü °£¿° c Ç׿ø
  • HBc antigen
    BÇü °£¿°¹ÙÀÌ·¯½º ÇÙ½ÉÇ׿ø
  • HBe Ag => hepatitis B e antigen
    B Çü °£¿° e Ç׿ø
  • HBe antigen
    BÇü °£¿°¹ÙÀÌ·¯½º eÇ׿ø
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  • ¿µ¹®
    ÇѱÛ
  • breathing capacity
    È£Èí¿ë·®(¡­é»åÖ)
  • buffering capacity
    ¿ÏÃæ´É(èÐõúÒö)
  • capacity
    ¿ëÀû, ·®, ´É·Â, ´É
  • cranial capacity
    µÎ°³³»¿ë·®(¡­Ò®é»åÖ).
  • diffusing capacity
    È®»ê´É
  • diffusing capacity
    È®»ê´É, È®»ê¼º ´É·Â(¡­Òöæ³).
  • diffusion capacity
    È®»ê´É(üªß¤Òö)
  • effective capacity
    À¯È¿¿ë·®.
  • electric capacity
    Àü±â¿ë·®(ï³Ñ¨é»Õá)
  • expiratory vital capacity =EVC
    È£½ÄÆóȰ·®(¡­øËüÀåÖ).
  • forced vital capacity
    °­Á¦ÆóȰ·®, ³ë·Â¼ºÆóȰ·®, ³ë¼ºÆóȰ·®
  • forced vital capacity =FVC
    °­Á¦ÆóȰ·®,³ë·Â¼º ÆóȰ·®, ³ë¼º ÆóȰ·®
  • forced vital capacity =FVC
    °­Á¦ÆóȰ·®(Ë­ð¤øËüÀÕá), ³ë·Â¼º ÆóȰ·®(Ò½æ³àõøËüÀåÖ), ³ë¼º?
  • forced vital capacity =FVC
    °­Á¦ÆóȰ·®, ³ë·Â¼º ÆóȰ·®(Ò½æ³àõ
  • functional capacity
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  • ¿µ¹®
    ÇѱÛ
  • complete antigen
    ¿ÏÀüÇ׿ø(èÇîïù÷ê«)
  • conjugated antigen
    Æ÷ÇÕÇ׿ø(øÙùêù÷ê«)
  • cross-reacting antigen
    ±³Â÷¹ÝÀÀ Ç׿ø(Îßó©Úãëëù÷ê«)
  • differentiation antigen
    ºÐÈ­ Ç׿ø(ÝÂûùù÷ê«)
  • Ea antigen
    Ea Ç׿ø(ù÷êª)
  • eclipsed antigen
    °¡¸² Ç׿ø (ù÷ê«)
  • fluorescent antigen
    Çü±¤ Ç׿ø(û«ÎÃù÷ê«)
  • H antigen
    H Ç׿ø(ù÷ê«)
  • haptenic antigen
    ÇÕÅÙ Ç׿ø(ù÷ê«)
  • hepatitis B surface antigen
    BÇü(úþ) °£¿°(ÊÜæú) Ç¥¸é Ç׿ø(øúØüù÷ê«)
  • heterogenetic antigen
    ÀÌÁ¾ Ç׿ø(ì¶ðúù÷ê«)
  • heterophile antigen
    ÀÌÈ£¼º Ç׿ø(ì¶û¿àõù÷ê«)
  • hexon antigen
    Çí¼Õ Ç׿ø(ù÷ê«)
  • histocompatibility antigen
    Á¶Á÷ÀûÇÕ¼º Ç׿ø(ðÚòÄîêùêàõù÷ê«)
  • Ia antigen
    Ia Ç׿ø(ù÷ê«)
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MSBC maximum specific binding capacity
SRCBC serum reserve cholesterol binding capacity
TIBC total iron-binding capacity
UBBC unsaturated vitamin B12 binding capacity
UIBC unsaturated iron-binding capacity
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IVC Inspiratory Vital Capacity
VmaxFRC Maximal flow at functional residual capacity
NACS Neurologic and Adaptive Capacity Score
ORAC Oxygen Radical Absorbance Capacity
PWC Physical Work Capacity
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • lymphocyte defined antigen
    ¸²ÇÁ±¸ ±ÔÁ¤ Ç׿ø
  • N-antigen
    N Ç׿ø
  • nuclear antigen
    ÇÙ Ç׿ø
  • pancreatic oncofetal antigen
    ÃéÀåÀÇ Å¾Ƽº ¾Ï Ç׿ø
  • pollen antigen
    ²É°¡·ç Ç׿ø, È­ºÐ Ç׿ø
  • polyvalent antigen
    ´Ù°¡ Ç׿ø
  • self antigen
    ÀÚ±â Ç׿ø
  • somatic antigen
    ±Õü Ç׿ø, ü¼¼Æ÷ Ç׿ø
  • treponema antigen test
    Æ®·¹Æ÷³×¸¶ Ç׿ø ½ÃÇè
  • tumor associated antigen
    ¾Ï °ü·Ã Ç׿ø
    ÀϺÎÀÇ Á¤»ó ¼¼Æ÷¿¡¼­¸¸ ¹ß°ßµÇ¾î ÀÖÀ¸³ª ¾Ï ¼¼Æ÷¿¡¼­µµ ¸¹Àº ¹üÀ§¿¡¼­ ¹ßÇöµÈ Ç׿ø, Á¤»ó ¼¼Æ÷¿¡¼­´Â ¹Ì·®ÀÌ Á¸ÀçÇϳª ¾Ï ¼¼Æ÷¿¡¼­´Â ´Ù·®ÀÌ °ËÃâµÇ´Â Ç׿ø, ±×·¯³ª °áÄÚ ¾Ï ƯÀÌÀûÀ̶ó°í ÇÒ ¼ö ¾ø´Â ¼ºÁúÀÇ Ç׿ø.
  • viral capsid antigen
    ¹ÙÀÌ·¯½º ĸ½Ãµå Ç׿ø, ¹ÙÀÌ·¯½º¼º ĸ½Ãµå Ç׿ø
  • virus bound antigen
    ¹ÙÀÌ·¯½º °áÇÕ Ç׿ø
  • virus-specific surface antigen
    ¹ÙÀÌ·¯½º ƯÀ̼º Ç¥¸é Ç׿ø ¹ÙÀÌ·¯½º
  • zone of antigen excess
    Ç׿ø °úÀ×´ë
    ºñ±³Àû °í³óµµÀÇ Ç׿ø´ë·Î¼­ ħ°­¹ÝÀÀ¿¡¼­ °¡¿ë¼º º¹ÇÕü°¡ Çü¼ºµÇ¸ç ¹ÝÀÀÀÌ ¾ïÁ¦µÈ´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 5
sex hormone-binding globulin A glycoprotein migrating as a beta-globulin. Its molecular weight, 52,000 or 95,000-115,000, indicates that it exists as a dimer. The protein binds testosterone, dihydrotestosterone, and estradiol in the plasma. Changes in its concentration significantly affect the ratio of unbound (biologically active) testosterone to estradiol in plasma.
(12 Dec 1998)
sex steroid-binding globulin A protein that transports 65% of the testosterone in plasma.
Synonym: sex steroid-binding globulin.
(05 Mar 2000)
single stranded binding protein <protein> SSB's are proteins responsiblefor holding the replication fork of DNAopen while polymerases readthe templates.
(09 Oct 1997)
Nuclear actin binding protein <molecular biology> Nuclear protein, dimer of 34 kD subunits. Binds actin with Kd of around 25M.
(18 Nov 1997)
nuclear binding energy <physics> The difference between the total energy (= mc^2) of the bound nucleus, and the energies of the individual constituent particles (= sum of masses c^2). The nuclear binding energy per nucleon is a maximum for iron. Fusion releases energy because light nuclei are less tightly bound than medium-weight nuclei, and thus energy is liberated when they become more tightly bound after fusing. Fission releases energy for the same reason - heavy nuclei are also less tightly bound than medium-weight nuclei, and energy is liberated when heavy nuclei split into lighter nuclei.
(09 Oct 1997)
nucleotide binding fold Protein motif consisting of a fold or pocket with certain conserved residues, required for the binding of nucleotides.
(18 Nov 1997)
DNA binding protein <molecular biology> Proteins that interact with DNA, typically to pack or modify the DNA for example histones or to regulate gene expression, transcription factors. Among those proteins that recognise specific DNA sequences, there are a number of characteristic conserved motifs believed to be essential for specificity.
(18 Nov 1997)
DNA-binding protein, cyclic AMP-responsive A protein that has been shown to function as a calcium regulated transcription factor as well as a substrate for depolarisation-activated calcium calmodulin-dependent protein kinases I and II. This protein functions to integrate both calcium and camp signals.
(12 Dec 1998)
DNA-binding proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
(12 Dec 1998)
insulin binding When insulin attaches itself to something else. This can occur in two ways. First, when a cell needs energy, insulin can bind with the outer part of the cell. The cell then can bring glucose (sugar) inside and use it for energy. With the help of insulin, the cell can do its work very well and very quickly. But sometimes the body acts against itself. In this second case, the insulin binds with antibodies. If the insulin is an injected form of insulin and not made by the body, the body sees the insulin as an outside or foreign substance. When the injected insulin binds with the antibodies, it does not work as well as when it binds directly to the cell.
(09 Oct 1997)
insulin-like growth-factor binding protein 1 One of the six homologous proteins that specifically bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions. The function of this protein is not completely defined. However, several studies demonstrate that it inhibits igf binding to cell surface receptors and thereby inhibits igf-mediated mitogenic and cell metabolic actions. (proc soc exp biol med 1993;204(1):4-29)
(12 Dec 1998)
insulin-like growth factor-binding protein 2 One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level.
(12 Dec 1998)
insulin-like growth factor binding protein 3 One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level.
(12 Dec 1998)
insulin like growth-factor-binding protein 4 One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level.
(12 Dec 1998)
insulin-like growth-factor-binding-protein 5 One of the six homologous soluble proteins that bind insulin-like growth factors (somatomedins) and modulate their mitogenic and metabolic actions at the cellular level.
(12 Dec 1998)
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