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  • ¿µ¹®
    ÇѱÛ
  • 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
  • factor XIII
    Á¦13ÀÎÀÚ
  • granulocyte colony-stimulating factor
    °ú¸³±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage colony-stimulating factor
    °ú¸³±¸Å«Æ÷½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ, °ú¸³±¸´ë½Ä±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • growth factor
    ¼ºÀåÀÎÀÚ
  • hyperglycemic-glycogenolytic factor
    °íÇ÷´ç±Û¸®ÄÚ°ÕºÐÇØÀÎÀÚ
  • hematopoietic growth factor
    Ç÷¾×Çü¼º¼ºÀåÀÎÀÚ, Á¶Ç÷¼ºÀåÀÎÀÚ
  • histamine sensitizing factor
    È÷½ºÅ¸¹Î¹Î°¨ÀÎÀÚ
  • host integration factor
    ¼÷ÁÖÅëÇÕÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢À¯¹ßÀÎÀÚ
  • dilution factor
    ¹±ÈûÀÎÀÚ, Èñ¼®ÀÎÀÚ
  • drug resistance factor
    ¾àÁ¦ÀúÇ×ÀÎÀÚ
  • elongation factor
    ´ÃÀÓÀÎÀÚ, ¿¬ÀåÀÎÀÚ
  • endothelium-derived contracting factor
    ³»ÇǼ¼Æ÷¼öÃàÀÎÀÚ
  • endothelium-derived relaxing factor
    ³»ÇǼ¼Æ÷ÀÌ¿ÏÀÎÀÚ
  • endurance factor
    Áö¼ÓÀÎÀÚ
  • eosinophil chemotactic factor
    È£»ê±¸È­ÇÐÁÖ¼ºÀÎÀÚ, È£»ê±¸È­Çнò¸²ÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ
  • exogenous factor
    ¿ÜÀοä¼Ò
  • extrinsic factor
    ¿ÜÀÎÀÎÀÚ, ¿ÜÀÎÀÚ
  • factor
    ÀÎÀÚ, ¿äÀÎ, °è¼ö
  • factor theory
    ¿äÀÎÀÌ·Ð
  • fermentation factor
    ¹ßÈ¿ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • age factor
    ¿¬·ÉÀÎÀÚ.
  • air kerma calibration factor
    °ø±âÄ¿¸¶ÃøÁ¤°è¼ö, -´«±Ý¸ÂÃã°è¼ö
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ(¡­ýüà·ì×í­).
  • amplification factor
    ÁõÆøÀÎÀÚ
  • anisotropy factor
    ºñµî¹æ¼º°è¼ö
  • antigen, colonization factor
    Áý¶ôÇü¼ºÀÎÀÚÇ׿ø, ¼¼Æ÷±ºÇü¼ºÀÎÀÚÇ׿ø
  • antihemophilic A factor =AHA
    Ç×Ç÷¿ìº´ AÀÎÀÚ(?ËöËö).
  • antihemophilic factor =AHF
    Ç×Ç÷¿ìº´ÀÎÀÚ(¡­ì×í­)
  • antihemophilic factor =AHF
    Ç×Ç÷¿ìº´ÀÎÀÚ(?ËöËö).
  • antihemophllic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antiinsulin factor
    Ç×Àν¶¸°ÀÎÀÚ.
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ(ù÷ãêÌèæúì×í­).
  • antinuclear factor =ANF
    Ç×ÇÙÀÎÀÚ.
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ.
  • antiphagocytic factor
    Ç׎½ÄÀÎÀÚ, Ç׽ıÕÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • recovery time
    ȸº¹ ±â°£, ȸº¹ ½Ã°£
  • reflex time
    ¹Ý»ç½Ã°£(ÚãÞÒãÁÊà).
  • relaxation time
    À̿Ͻð£ (ì¬èÐãÁÊà)
  • relaxation time
    ÀÌ¿Ï ½Ã°£
  • relaxation time
    À̿Ͻð£(ì¬èÐãÁÊà).
  • repetition time (TR)
    ¹Ýº¹ ½Ã°£
  • retention time
    Á¤Ã¼½Ã°£
  • reverberation time
    ÀÜÇâ½Ã°£(íÑúÂãÁÊà).
  • ring down time
    ¿©¿î ½Ã°£ (æ®ê¤ ãÁÊà)
  • ring down time
    ¿©¿î ½Ã°£)
  • rise time
    »ó½Â ½Ã°£
  • rising time
    »ó½Â ½Ã°£
  • scan time
    ÁÖ»ç½Ã°£
  • sedimentation time
    ħ°­½Ã°£( ˽ãÁÊà).
  • sensitive time
    °¨ÀÀ½Ã°£(ÊïëëãÁÊà).
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  • ¿µ¹®
    ÇѱÛ
  • integration host factor
    ÅëÇÕ ¼÷ÁÖÀÎÀÚ(÷ÖùêâÖñ«ì×í­)
  • intrinsic factor
    ³»ÀÎÀÎÀÚ(Ò®ì×ì×í­)
  • labile factor
    ºÒ¾ÈÁ¤ÀÎÀÚ(ÝÕäÌïÒì×í­)
  • Laki-Lorand factor
    ¶óŰ-·Î¶õµå ÀÎÀÚ(ì×í­)
  • Lande G factor
    ¶õµ¥ G ÀÎÀÚ(ì×í­)
  • lard factor
    µ·Áö(ÔÊò·) ÀÎÀÚ(ì×í­)
  • leukocyte inhibitory factor
    ¹éÇ÷±¸ÀúÇØÀÎÀÚ(ÛÜúìϹîÁúªì×í­)
  • Lewis factor
    ·çÀ̽ºÀÎÀÚ(ì×í­)
  • lipoprotein tissue factor
    ÁöÁú´Ü¹éÁú(ò·òõÓ±ÛÜòõ) Á¶Á÷ÀÎÀÚ(ðÚòÄì×í­)
  • liver filtrate factor
    °£ ¿©°ú ÀÎÀÚ(ÊÜÕëΦì×í­)
  • LLD factor
    LLD ÀÎÀÚ(ì×í­)
  • L-L factor
    "L-L ÀÎÀÚ(ì×í­), (å²) Laki-Lorand ÀÎÀÚ(ì×í­)"
  • lymph node permeability factor
    ¸²ÇÁÀý(ï½)Åõ°úÀÎÀÚ(÷âΦì×í­)
  • lymphocyte-derived chemotactic factor
    ¸²ÇÁ±¸-À¯µµ(ë¯Óô) È­ÇÐÁÖ¼ºÀÎÀÚ(ûùùÊñËà÷ì×í­)
  • macrophage activation factor
    ´ë½Ä¼¼Æ÷Ȱ¼ºÀÎÀÚ(ÓÞãÝá¬øàüÀàõì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
a.t. acquisition time; ¿µ»óȸº¹½Ã°£
  = TR x N x Nex
  TR; Time to Repeat
 &...
ART absolute retention time; Accredited Record Technician; acoustic reflex test; algebraic reconstructio...
BLT bleeding time; blood-clot lysis time; blood test
CLT Certified Laboratory Technician; chronic lymphocytic thyroiditis; Clinical Laboratory Technician; cl...
CTT cefotetan; central tegmental tract; central transmission time; compressed tablet triturate; computer...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
ECT Ecarin Clotting Time
ETI Ejection time index
ECLT Euglobulin Clot Lysis time
ELT Euglobulin Lysis Time
FCT Fever clearance time
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • factor IX deficiency
    Á¦ 9ÀÎÀÚ °áÇÌÁõ, Á¦9ÀÎÀÚ °áÇÌ
  • factor macrophage migration inhibition
    ´ë½Ä ¼¼Æ÷ À¯ÁÖ ÀúÁö ÀÎÀÚ
  • factor VII deficiency
    Á¦ 7ÀÎÀÚ °áÇÌÁõ
  • factor VIII deficiency
    Á¦ 8ÀÎÀÚ °áÇÌ
  • factor XI deficiency
    Á¦11ÀÎÀÚ °áÇÌ
    ÀÌ ÀÎÀÚ°¡ ºÎÁ·µÇ¸é Ç÷¿ìº´ C³ª Rosenthal ÁõÈıºÀ¸·Î ºÒ¸®´Â Àü½Å¼º Ç÷¾× ÀÀ°í Àå¾Ö¸¦ ÀÏÀ¸Å°´Âµ¥ °íÀüÀû Ç÷¿ìº´°ú À¯»çÇÏ´Ù.
  • follicle stimulating hormone releasing factor
    ³­Æ÷ ÀÚ±Ø È£¸£¸ó ¹æÃâ ÀÎÀÚ
  • Hageman factor
    ÇϰԸ¸ ÀÎÀÚ
    factor ?.
  • hormonal factor
    È£¸£¸ó ¿äÀÎ
  • hunter blood factor
    ÇåÅÍ Ç÷¾× ÀÎÀÚ
  • hypoglycemic producing factor
    ÀúÇ÷´çÁõ À¯¹ß ¿äÀÎ
  • hypophosphatemia-producing factor

    hypophosphatemic rickets (ÀúÀλê Ç÷¼º ±¸·çº´, ÀúÀλ꿰 Ç÷¼º ±¸·çº´

  • initiating factor
    À¯¹ß ¿äÀÎ
    ÁúȯÀ̳ª Àå¾ÖÀÇ ¹ßº´¿¡ ¿øÀÎÀÌ µÇ´Â ¿ä¼Òµé.
  • intrinsic factor antibody
    ³»Àμº ÀÎÀÚ Ç×ü
  • irritating factor
    ÀÚ±Ø ¿ä¼Ò
  • labile factor
    ºÒ¾ÈÁ¤ ÀÎÀÚ, ºÒ¾ÈÁ¤ ¿ä¼Ò
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
mammotropic factor <protein> Pituitary lactogenic hormone (23 kD) Synthesised on endoplasmic reticulum bound ribosomes as preprolactin that has an N terminal signal peptide that is cleaved from the mature form. The conversion of preprolactin to prolactin has been much used as an assay for membrane insertion.
(18 Nov 1997)
receptors, atrial natriuretic factor Cell surface proteins that bind atrial natriuretic factor with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, colony-stimulating factor Cell surface receptors for colony-stimulating factors, local mediators, and hormones that regulate the survival, proliferation, and differentiation of haemopoietic cells.
(12 Dec 1998)
receptors, epidermal growth factor-urogastrone Glycoproteins of about 170 kD that have protein kinase activity and span the plasma membranes of growing cells, including tumours. They are activated by the binding of epidermal growth factor-urogastrone which then initiates DNA and protein synthesis. They are not found on mitotically quiescent cells except in the stomach where they control the synthesis and release of digestive enzymes and gastric acid. Transforming growth factor alpha also binds to and activates these receptors.
(12 Dec 1998)
receptors, fibroblast growth factor Specific molecular sites or structures on cell membranes that react with fibroblast growth factors (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity.
(12 Dec 1998)
receptors, granulocyte-colony-stimulating factor Receptors that bind and internalise granulocyte-colony-stimulating factor. Their mw is believed to be 150 kD. These receptors are found mainly on a subset of myelomonocytic cells.
(12 Dec 1998)
receptors, granulocyte-macrophage colony-stimulating factor Receptors that bind and internalise the granulocyte-macrophage stimulating factor. Their mw is believed to be 84 kD. The most mature myelomonocytic cells, specifically human neutrophils, macrophages, and eosinophils, express the highest number of affinity receptors for this growth factor.
(12 Dec 1998)
receptors, growth factor Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.
(12 Dec 1998)
receptors, insulin-like-growth factor I Specific proteins on or in cells to which insulin-like growth factor I (somatomedin c) binds and thereby modifies the function of the cells. These receptors contain transmembrane and cytosolic domains, bind igf-I preferentially, and have high-affinity sites for igf-II. The alpha-subunit has a mw of 130 kD and the beta subunit possesses tyrosine kinase activity.
(12 Dec 1998)
receptors, insulin-like-growth-factor II Specific proteins on or in cells to which insulin-like growth factor II and mannose-6-phosphate bind and thereby modify the function of the cells. These receptors have a mw of 250 kD and possess no tyrosine kinase activity.
(12 Dec 1998)
receptors, macrophage colony-stimulating factor Glycoproteins of mw 165 kD which are encoded by the c-fms proto-oncogene. The binding of csf-1 to its receptors activates an intrinsic tyrosine kinase activity resulting in autophosphorylation of the receptors on tyrosine, rapid receptor down-regulation, and phosphorylation of as yet unidentified physiologic substrates that initiate a mitogenic response.
(12 Dec 1998)
receptors, nerve growth factor Cell surface receptors that bind nerve growth factor (ngf) and trigger intracellular changes influencing the behaviour of cells. Nerve growth factor receptors mediate the effects of nerve growth factor on the survival and growth of neurons.
(12 Dec 1998)
receptors, platelet-derived growth factor Specific molecular sites or structures on cell membranes that react with platelet-derived growth factor, its analogs, or antagonists, to elicit or to inhibit the specific response of the cell to this factor. Pdgf binds with different affinities and specificities to two structurally related receptors, the alpha-receptor and the beta-receptor. Both of these receptors are transmembrane proteins with an intracellular, ligand-stimulatable protein kinase domain.
(12 Dec 1998)
receptors, transforming growth factor beta Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behaviour of cells. Two types of transforming growth factor receptors have been recognised. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action. Transforming growth factor alpha binds to the same receptors as epidermal growth factor (see receptors, epidermal growth factor-urogastrone).
(12 Dec 1998)
receptors, tumour necrosis factor Cell surface receptors that bind tumour necrosis factor and trigger changes which influence the behaviour of cells. The two recognised tumour necrosis factor receptors are designated alpha and beta receptors. Both receptors bind both alpha and beta tumour necrosis factors with high affinity, and both are members of the nerve growth factor receptor family.
(12 Dec 1998)
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  • ¿µ¹®
    ÇѱÛ
  • time card
    Áý¹« ½Ã°£ Ä«µå;±âÂ÷ ½Ã°£Ç¥
  • time charter
    Á¤±â ¿ë¼± °è¾à
  • time deposit
    Á¤±â ¿¹±Ý
  • time draft
    À϶÷ºÒ Á¤±â ¾îÀ½
  • time exposure
    ŸÀÓ ³ëÃâ(ÀÇ »çÁø)
  • time killer
    ½É½ÉÇ®À̰¡ µÇ´Â°Í
  • time lag
    ½Ã°£ÀÇ ¾î±ß³²;Áöü(·®)
  • time limit
    ½ÃÇÑ
  • time machine
    ŸÀӸӽŠ(°ú°Å³ª ¹Ì·¡¸¦ ¿©ÇàÇϱâ À§ÇÑ »ó»ó»óÀÇ ±â°è)
  • time note
    ¾à¼Ó¾îÀ½
  • time recorder
    ŸÀÓ ·¹ÄÚ´õ 6
  • time sharing
    (ÄÄÇ»ÅÍ) ŸÀÓ ¼Î¾î¸µ;½Ã¹èºÐ(¹æ½Ä)
  • time signal
    ½Ãº¸
  • time signature
    ¹ÚÀÚ±âÈ£
  • time sprit
    ½Ã´ëÁ¤½Å
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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