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"animal protein factor"¿¡ ´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
  • dilution factor
    Èñ¼®ÀÎÀÚ
  • exclusion of confounding factor
    ±³¶õ¹èÁ¦ÀÎÀÚ
  • exogenous factor
    ¿ÜÀοä¼Ò
  • extrinsic factor
    ¿ÜÀÎÀÎÀÚ, ¿ÜÀÎÀÚ
  • elongation factor
    ´ÃÀÓÀÎÀÚ, ¿¬ÀåÀÎÀÚ
  • endothelium-derived contracting factor
    ³»ÇÇÀ¯·¡¼öÃàÀÎÀÚ
  • endothelium-derived relaxing factor
    ³»ÇÇÀ¯·¡ÀÌ¿ÏÀÎÀÚ
  • endurance factor
    °ßµõÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ
  • fermentation factor
    ¹ßÈ¿ÀÎÀÚ
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • fermentation factor
    ¹ßÈ¿ÀÎÀÚ
  • fertility factor
    ¼öÅÂÀÎÀÚ
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • 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)
  • Factor VII
    VII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor VIII
    VIII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor X activated
    Ȱ¼ºÈ­(üÀàõûù)µÈ X ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor XI
    XI ÀÀ°íÀÎÀÚ(ëêͳì×í­)
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  • ¿µ¹®
    ÇѱÛ
  • iron porphyrin protein enzymes
    öÆ÷¸£ÇǸ°´Ü¹éÈ¿¼Ò(¡­Ó±ÛÜý£áÈ).
  • iron-sulfur protein
    ÀüÀÚÀü´Þ ö-À¯È²´Ü¹éÁú
  • liver membrane protein
    °£¸·´Ü¹é
  • liver specific protein
    °£Æ¯À̴ܹé
  • low protein diet
    Àú´Ü¹é½Ä(î¸Ó±ÛÜãÝ).
  • maintenance protein
    À¯Áö´Ü¹éÁú(¡­Ó±ÛÜòõ).
  • major basic protein
    ÁÖ±âÀú´Ü¹é
  • major basic protein
    ÁÖ¿ä ±âÃʴܹé(ñ«é© Ðñõ¨Ó±ÛÜ)
  • matrix protein
    ±âÁú´Ü¹éÁú
  • membrane control protein
    ¸·Á¶Àý´Ü¹é
  • mitogen-activated protein kinase
    ¹ÌÅä°Õ Ȱ¼º ´Ü¹é ±Í³ªÁ¦(¡­ üÀàõ Ó±ÛÜ ¡­ )
  • monocyte chemotactant protein 1(mcp-1)
    ´Ü±¸È­ÇÐÁÖ¼º´Ü¹é(¡­ûùùÊñ«àõÓ±ÛÜ) 1 (MCP-1)
  • muscle protein
    ±Ù´Ü¹é(ÐÉÓ±ÛÜ).
  • myelin basic protein
    ¼öÃÊ(âÐÃÊ)¿°±â¼º ´Ü¹é
  • myelin basic protein
    ¸¶ÀÌ¿¤¸° ¿°±â´Ü¹éÁú
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  • ¿µ¹®
    ÇѱÛ
  • initiation factor
    °³½ÃÀÎÀÚ(ËÒã·ì×í­)
  • instability factor
    ºÒ¾ÈÁ¤ÀÎÀÚ(ÝÕäÌïÒì×í­)
  • 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)
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ABP actin-binding protein; ambulatory blood pressure; American Board of Pedodontics; American Board of P...
CBP calcium-binding protein; carbohydrate-binding protein; cardiopulmonary bypass; chlorobiphenyl; cobal...
CP candle power; capillary pressure; cardiac pacing; cardiac performance; cardiopulmonary; caudate puta...
CRP chronic relapsing pancreatitis; corneal-retinal potential; coronary rehabilitation program; C-reacti...
CSP carotid sinus pressure; cavum septi pellucidi; cell surface protein; cerebrospinal protein; Chartere...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 8
G-protein Guanine nucleotide-binding protein
r-protein Ribosomal protein
SSB-protein Single-stranded DNA-binding protein
G protein binding protein
M protein monoclonal protein
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 8
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 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
  • EDA : electronic dental anesthesiaÀÇ ¾àÀÚ.

    edaphic factor

    ÅäÁö ÀÎÀÚ
  • effector-inhibitory factor
    È¿°ú±â ¾ïÁ¦ ÀÎÀÚ
  • emotional factor
    Á¤¼­ ¿äÀÎ
  • enabling factor
    ÀÇ·á ÀÌ¿ë °¡´É ¿äÀÎ
  • endogenous factor
    ³»Àμº ¿ä¼Ò
  • endothelium-derived relaxing factor
    ³»ÇÇ ¼¼Æ÷¼º ÀÌ¿Ï ÀÎÀÚ
  • endurance factor
    Áö¼Ó ÀÎÀÚ
  • environmental chemotactic factor
    ȯ°æ¼º È­ÇÐ ÁÖ¼º ÀÎÀÚ
  • eosinophil chemotactic factor
    È£»ê±¸ È­ÇÐ ÁÖ¼º ÀÎÀÚ
  • excess factor
    °úÀ× ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 8
vascular endothelial growth factor A growth factor that is responsible for the growth of blood vessels.
(12 Dec 1998)
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)
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    ±¸ºÐ/º¸Çè±Þ¿©
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