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  • ¿µ¹®
    ÇѱÛ
  • fertility factor
    ¼öÅÂÀÎÀÚ
  • fibrin stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ
  • fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷¼ºÀåÀÎÀÚ
  • factor
    1. ÀÎÀÚ 2. ¿äÀÎ 3. °è¼ö
  • factor III
    Á¦3ÀÎÀÚ
  • factor IV
    Á¦4ÀÎÀÚ
  • factor IX
    Á¦9ÀÎÀÚ
  • factor IX complex
    Á¦9ÀÎÀÚº¹ÇÕü
  • factor V
    Á¦5ÀÎÀÚ
  • factor VI
    Á¦6ÀÎÀÚ
  • factor VII
    Á¦7ÀÎÀÚ
  • factor VIII
    Á¦8ÀÎÀÚ
  • factor X
    Á¦10ÀÎÀÚ
  • factor XI
    Á¦11ÀÎÀÚ
  • factor XII
    Á¦12ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • fibrin stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ
  • fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷¼ºÀåÀÎÀÚ
  • granulocyte colony-stimulating factor
    °ú¸³±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage colony-stimulating factor
    °ú¸³±¸Å«Æ÷½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ
  • growth factor
    ¼ºÀåÀÎÀÚ
  • hematopoietic growth factor
    Ç÷¾×Çü¼º¼ºÀåÀÎÀÚ, Á¶Ç÷¼ºÀåÀÎÀÚ
  • histamine sensitizing factor
    È÷½ºÅ¸¹Î¹Î°¨ÀÎÀÚ
  • host integration factor
    ¼÷ÁÖÅëÇÕÀÎÀÚ
  • hyperglycemic-glycogenolytic factor
    °íÇ÷´ç±Û¸®ÄÚ°ÕºÐÇØÀÎÀÚ
  • insulin-like growth factor
    Àν¶¸°À¯»ç¼ºÀåÀÎÀÚ
  • intrinsic factor
    ³»ÀÎÀÎÀÚ, ³»ÀÎÀÚ
  • ketogenic factor
    ÄÉÅæÇü¼ºÀÎÀÚ
  • labile factor
    ºÒ¾ÈÁ¤ÀÎÀÚ, ºÒ¾ÈÁ¤¿ä¼Ò
  • lactogenic factor
    Á¥ÃËÁøÀÎÀÚ
  • leukocyte inhibitory factor
    ¹éÇ÷±¸¾ïÁ¦ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • B cell growth factor
    B ¼¼Æ÷¼ºÀåÀÎÀÚ
  • B cell growth factor (BCGF)
    B¼¼Æ÷ Áõ½ÄÃËÁøÀÎÀÚ
  • B cell stimulating factor (BSF)
    B¼¼Æ÷ ÀÚ±ØÀÎÀÚ
  • Castles extrinsic factor
    Ĺ½½¿ÜÀÎÀÚ.
  • Castles intrinsic factor
    Ĺ½½³»ÀÎÀÚ.
  • Christmas factor
    Å©¸®½º¸¶½º ÀÎÀÚ(ì×í­)
  • Christmas factor.
    Å©¸®½º¸¶½ºÀÎÀÚ
  • D factor
    DÀÎÀÚ
  • Decay accelerating factor
    ºØ±«°¡¼Ó¿ä¼Ò(¿äÀÎ)
  • EDCF (endothlium-derived contracting factor)
    ³»ÇǼ¼Æ÷¼º(Ò®ù«á¬øààõ) ¼öÃàÀÎÀÚ(â¥õêì×í­)
  • EDRF (endothlium-derived relaxing factor)
    ³»ÇǼ¼Æ÷¼º(Ò®ù«á¬øààõ) ÀÌ¿ÏÀÎÀÚ(ì¬èÐì×í­)
  • EDRF=£¾endothelium derived relaxing factor
    ³»ÇǼ¼Æ÷¼ºÀÌ¿ÏÀÎÀÚ.
  • F factor
    FÀÎÀÚ
  • Factor IX
    IX ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor V
    V ÀÀ°íÀÎÀÚ(ëêͳì×í­)
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  • ¿µ¹®
    ÇѱÛ
  • alpha blocking
    ¾ËÆÄÂ÷´Ü
  • alpha cell
    ¾ËÆÄ¼¼Æ÷
  • alpha cell
    ¾ËÆÄ¼¼Æ÷(¡­á¬øà)
  • alpha cell glucagon cell
    ¾ËÆÄ¼¼Æ÷ ±Û·çÄ«°ï¼¼Æ÷
  • alpha cell tumor
    ¾ËÆÄ ¼¼Æ÷Á¾(¡­á¬øàðþ)
  • alpha chain disease
    ¾ËÆÄ¼âº´(¡­áðÜ»).
  • alpha chain disease
    ¾ËÆÄ¼âÁúȯ
  • alpha cradle
    ¾ËÆÄ¹Þħ´ë
  • alpha decay
    ¾ËÆÄºØ±«
  • alpha emitter
    ¾ËÆÄ¹æ»çü, ¾ËÆÄ¹æÃâü
  • alpha fetoprotein =AFP
    ¾ËÆÄžƴܹé(¡­÷Ãä®Ó±ÛÜ).
  • alpha fiber
    ¾ËÆÄ(½Å°æ)¼¶À¯
  • alpha granule
    ¾ËÆÄ °ú¸³(¡­Î¨Ø£)
  • alpha hemolysis
    ¾ËÆÄ¿ëÇ÷(¡­éÁúì).
  • alpha hemolysis
    ¾ËÆÄ¿ëÇ÷(¡­éÁúì).
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  • ¿µ¹®
    ÇѱÛ
  • antinuclear factor
    Ç×ÇÙÀÎÀÚ(ù÷ú·ì×í­)
  • antipellagra factor
    Ç×(ù÷)Æç¶ó±×¶ó ÀÎÀÚ(ì×í­)
  • antipeptic ulcer factor
    Ç×(ù÷)±Ë¾ç(Ï÷åË) ÀÎÀÚ(ì×í­)
  • antipernicious anemia factor
    Ç×(ù÷)¾Ç¼ººóÇ÷(äÂàõÞ¸úì) ÀÎÀÚ(ì×í­)
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ(ù÷ÎÕúìÜ»ì×í­)
  • antisigma factor
    Ç×(ù÷)½Ã±×¸¶ ÀÎÀÚ(ì×í­)
  • antispecificity factor
    Çׯ¯À̼º ÀÎÀÚ(ù÷÷åì¶àõì×í­)
  • antisterility factor
    Ç׺ÒÀÓ ÀÎÀÚ(ù÷ÝÕìõì×í­)
  • antitermination factor
    Ç×Á¾·á ÀÎÀÚ(ù÷ðûÖõì×í­)
  • antixerophthalmic factor
    Ç׾ȱ¸ °ÇÁ¶Áõ ÀÎÀÚ(ù÷äÑϹËëðÏñøì×í­)
  • Arrenius factor
    ¾Æ·¹´Ï¿ì½º ÀÎÀÚ(ì×í­)
  • asymmetry factor
    ºñ±¸»ó ÀÎÀÚ (ުϹßÒì×í­)
  • atrial natriuretic factor
    ½É¹æ(ãýÛ®) ³ªÆ®·ý¹è¼³ÀÎÀÚ(ÛÉàÜì×í­)
  • bacteriocin factor
    "¹ÚÅ׸®¿À½Å ÀÎÀÚ(ì×í­), »ì±ÕÀÎÀÚ(߯жì×í­)"
  • calcium-activated factor
    Ä®½·ºÎȰ ÀÎÀÚ(Ý·üÀì×í­)
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HBc, HBC, HBc hepatitis B core [antigen]
HBcAg, HBcAg, HBCAG hepatitis B core antigen
UQCRC ubiquinol-cytochrome C reductase core
OTF octamer-binding transcription factor; oral transfer factor
alpha-GLUC alpha-glucosidase
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anti-HBc Antibodies to hepatitis B core antigen
anti HBc Antibody to hepatitis B core antigen
CCD Central Core Disease
CC Coat-Core
CAPIT Core Assessment Program for Intracerebral Transplantation
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    ÇѱÛ
    ¼³¸í
  • coronary risk factor
    °ü»ó µ¿¸Æ Áúȯ À§Çè ¿äÀÎ
  • cothromboplastin factor VII
    ÄÚÆ®·Ò º¸ÇÃ¶ó½ºÆ¾
  • coupling factor
    ¹è¿ì ÀÎÀÚ
  • covering factor
    ÇǺ¹ ÀÎÀÚ
  • cultural and ethnic factor
    ¹®È­ ¹ÎÁ·Àû ¿äÀÎ
  • cytotoxic factor
    ¼¼Æ÷ µ¶¼º ÀÎÀÚ
  • D and C ÀÚ±ÃÀÇ °æºÎ È®Àå°ú ³»¸· ¼ÒÆÄ.

    D factor

    D-ÀÎÀÚ
  • Decay accelerating factor
    ºØ±« °¡¼Ó ¿ä¼Ò
  • diabetogenic factor
    ´ç´¢ À¯¹ß ÀÎÀÚ
  • differentiation factor
    °¨º° ¿äÀÎ, °¨º° ¿ä¼Ò, °¨º° ÀÎÀÚ
  • diffusion factor
    È®»ê ÀÎÀÚ
  • dilution factor
    Èñ¼® ÀÎÀÚ
  • dose modifying factor
    ¼±·® ¼ö½Ä °è¼ö
  • drug resistance factor
    ¾àÁ¦ ³»¼º ÀÎÀÚ
  • drug resistance transfer factor
    ¾àÁ¦ ³»¼º Àü´Þ ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
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)
intestinal calcium-binding protein <protein> Calcium-binding proteins containing the EF hand motif, induced by vitamin D3.
(18 Nov 1997)
iron-binding capacity The capacity of iron-binding protein in serum (transferrin) to bind serum iron.
(05 Mar 2000)
octamer binding protein <protein> Transcription factor that binds to the octamer motif.
Examples: mammalian proteins Oct 1, Oct 2.
(18 Nov 1997)
odourant binding protein Proteins in nasal mucus that bind lipophilic odour-producing molecules and transfer them to the olfactory receptors. Similar proteins may mediate taste.
(05 Mar 2000)
testosterone-oestrogen-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)
thyroid binding globulin <protein> Thyroid binding globulin (TBG) is a plasma protein which binds the majority of thyroid hormone in the bloodstream. Bound thyroid hormone is inactive, only the unbound fraction (0.3%) is considered active. Birth control pills and pregnancy can lead to increased TBG levels in the plasma. Androgens can decrease TBG levels in the plasma.
(27 Sep 1997)
thyroxine-binding globulin An alpha-globulin of blood with a strong binding affinity for thyroxine; triiodothyronine is bound to it much less firmly; a deficiency or excess of this protein may occur as a rare benign X-linked disorder.
Synonym: thyroxine-binding protein.
(05 Mar 2000)
thyroxine-binding protein An alpha-globulin of blood with a strong binding affinity for thyroxine; triiodothyronine is bound to it much less firmly; a deficiency or excess of this protein may occur as a rare benign X-linked disorder.
Synonym: thyroxine-binding protein.
(05 Mar 2000)
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