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"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
  • antihemophilic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ
  • antiphagocytic factor
    Çׯ÷½ÄÀÎÀÚ, Ç׎½ÄÀÎÀÚ
  • antiplatelet factor
    Ç×Ç÷¼ÒÆÇÀÎÀÚ
  • antirachitic factor
    Ç×±¸·çº´ÀÎÀÚ
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ
  • atrial natriuretic factor
    ½É¹æ³ªÆ®·ýÀÌ´¢ÀÎÀÚ, ½É¹æ¼ÒµãÀÌ´¢ÀÎÀÚ
  • activation factor
    Ȱ¼ºÀÎÀÚ
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ, ÇãÆÄ²Ê¸®Èñ¼®ÀÎÀÚ
  • amplification factor
    ÁõÆøÀÎÀÚ
  • behavioral risk factor
    ÇൿÀ§Çè¿äÀÎ
  • coagulation factor
    ÀÀ°íÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • colonizing factor antigen
    Áý¶ôÇü¼ºÀÎÀÚÇ׿ø
  • behavioral risk factor
    ÇൿÀ§Çè¿äÀÎ
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ
  • chemotactic factor
    È­ÇÐÁÖ¼ºÀÎÀÚ, È­Çнò¸²ÀÎÀÚ
  • coagulation factor
    ÀÀ°íÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°íÀÎÀÚ¾ïÁ¦Á¦
  • colony-stimulating factor
    Áý¶ôÀÚ±ØÀÎÀÚ
  • common factor
    °øÅëÀÎÀÚ
  • competence factor
    Àû°ÝÀÎÀÚ
  • competence inducing factor
    Àû°ÝÀ¯¹ßÀÎÀÚ
  • complementary factor
    º¸ÃæÀÎÀÚ, º¸Ã¼ÀÎÀÚ
  • conglutinogen activating factor
    ±³Âø¿øÈ°¼ºÀÎÀÚ
  • conversion factor
    º¯È¯ÀÎÀÚ, º¯È¯°è¼ö
  • corticotropin releasing factor
    ºÎ½Å°ÑÁúÀÚ±ØÈ£¸£¸ó¹æÃâÀÎÀÚ
  • decay accelerating factor
    ºØ±«ÃËÁøÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • protein 4.1
    ´Ü¹é 4.1
  • protein A
    ´Ü¹éÁú A (Æ÷µµ±¸±ÕÀÇ)
  • protein C
    C ´Ü¹é
  • protein score
    ´Ü¹é°¡(ËÀËÑ˧) ½ÄǰÀÇ .
  • protein sensitization
    ´Ü¹é°¨ÀÛ(¡­ÊïíÂ).
  • protein separation
    ´Ü¹éºÐ¸®
  • protein sparing effect
    ´Ü¹éÁúÀý¾àÈ¿°ú(Ó±ÛÜòõï½å³üùÍý).
  • protein synthesis
    ´Ü¹éÁúÇÕ¼º.
  • protein therapy
    ´Ü¹é(Áú)¿ä¹ý(¡­èþÛö).
  • protein,actin-binding
    ¾×ƾ-°áÇÕ(´Ü¹é)
  • protein,al
    AL(´Ü¹é)
  • protein,bence jones
    º¥½º-Á¸½º(´Ü¹é)
  • protein-calorie deficiency
    ´Ü¹é(Áú)¿­·®°áÇÌ(Ó±ÛÜ(òõ)æðÕáÌÀù¹)
  • protein-calorie malnutrition
    ´Ü¹é(Áú)¿­·®¿µ¾ç½ÇÁ¶(Áõ)(Ó±ÛÜ(òõ)æðÕáç½å×ã÷ðà(ñø))
  • protein-energy malnutrition
    ´Ü¹é(Áú)¿¡³ÊÁö¿µ¾ç½ÇÁ¶(Áõ)(¡­ç½å×ã÷ðà(ñø))
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  • ¿µ¹®
    ÇѱÛ
  • immune protein
    ¸é¿ª´Ü¹éÁú.
  • inner membrane protein
    ³»¸·´Ü¹éÁú
  • insoluble protein
    ºÒ¿ë¼º ´Ü¹é(Áú).
  • iodized protein
    ¿äµåÈ­´Ü¹éÁú(¡­Ó±ÛÜòõ).
  • iron binding protein =IBP
    ö°áÇÕ ´Ü¹éÁú.
  • iron porphyrin protein
    öÆ÷¸£ÇǸ°´Ü¹éÁú.
  • iron porphyrin protein
    ö(ôÑ)Æ÷¸£ÇǸ°´Ü¹éÁú(Ó±ÛÜòõ).
  • 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)
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  • ¿µ¹®
    ÇѱÛ
  • factor ¥³
    ÀÎÀÚ(ì×í­) IV
  • factor ¥´
    ÀÎÀÚ(ì×í­) V
  • factor ¥¶
    ÀÎÀÚ(ì×í­) VII
  • factor ¥·
    ÀÎÀÚ(ì×í­) VIII
  • factor ¥¸
    ÀÎÀÚ(ì×í­) IX
  • factor ¥¹
    ÀÎÀÚ(ì×í­) X
  • factor XI
    ÀÎÀÚ(ì×í­) XI
  • factor XII
    ÀÎÀÚ(ì×í­) XII
  • factor XIII
    ÀÎÀÚ(ì×í­) XIII
  • factor XIV
    ÀÎÀÚ(ì×í­) XIV
  • factor F
    ÀÎÀÚ(ì×í­) F
  • factor G
    ÀÎÀÚ(ì×í­) G
  • factor IF
    ÀÎÀÚ(ì×í­) IF
  • factor R
    ÀÎÀÚ(ì×í­) R
  • factor T
    ÀÎÀÚ(ì×í­) T
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EPF early pregnancy factor; endocarditis parietalis fibroplastica; endothelial proliferating factor; est...
HF Hageman factor; haplotype frequency; hard filled [capsule]; hay fever; head of fetus; head forward; ...
IF idiopathic fibroplasia; idiopathic flushing; immersion foot; immunofluorescence; indirect fluorescen...
KAF conglutinogen-activating factor; killer-assisting factor; kinase activating factor
LEF leukokinesis-enhancing factor; lupus erythematosus factor; lymphoid-enhanced binding factor
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 5
IGFBP-3 Insulin-like growth factor binding protein-3
IGFBP-1 Insulin-like growth factor (IGF)-binding protein 1
IGFBP-3 Insulin-like growth factor (IGF)-binding protein-3
IGF-BP insulin-like growth factor I and its binding protein
IGFBP-2 Insulin-like growth factor binding protein 2
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • chamber calibration factor
    Àü¸®ÇÔ ÃøÁ¤ °è¼ö, »óÀÚ ÃøÁ¤ °è¼ö
  • circumstance factor
    »óȲ ÀÎÀÚ
  • clotting factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • clumping factor
    ÀÀ±« ÀÎÀÚ
  • coagulase-reacting factor
    Ç÷Àå ÀÀ°í È¿¼Ò ¹ÝÀÀ ÀÎÀÚ
  • coagulation factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°í ÀÎÀÚ ¾ïÁ¦Á¦
  • colicin factor
    Äݸ®½Å ÀÎÀÚ
  • colony stimulating factor
    ±ºÃ¼ ÀÚ±Ø ¿ä¼Ò, Áý¶ô ÀÚ±Ø ÀÎÀÚ
    ¹ß´Þ ´Ü°èÀÇ Àü±¸Àû ¼¼Æ÷°¡ Áý¶ôÀ» Çü¼ºÇÏ´Â °úÁ¤¿¡´Â À̰ÍÀÇ ÀÛ¿ëÀÌ ÇÊ¿äÇÏ´Ù´Â °ÍÀÌ ÀνĵǾú´Ù. ÀÌ ÀÎÀÚ´Â ¼¶À¯¾Æ¼¼Æ÷, ³»ÇǼ¼Æ÷, ´ë½Ä¼¼Æ÷ µî¿¡¼­ »ý»êµÇ¸ç ¼º¼÷ÇÑ ¸é¿ª°è ¼¼Æ÷ÀÇ ÀÛ¿ë¿¡µµ ¿µÇâÀ» ³¢Ä£´Ù.
  • competence inducing factor
    Àû°Ý À¯¹ß ÀÎÀÚ
  • complementary factor
    º¸Ãæ ÀÎÀÚ
  • complicating factor
    º¹ÇÕ ¿äÀÎ
  • constitutional factor
    ±¸¼º ¿ä¼Ò, üÁú ¿äÀÎ
  • contributing factor
    ±â¿© ¿äÀÎ
    ÁúȯÀ̳ª Àå¾Ö¸¦ À¯¹ßÇϰųª ¾ÇÈ­Çϴµ¥ ±â¿©ÇÏ´Â »óųª Çൿ.
  • conversion factor
    º¯È¯ °è¼ö
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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)
G factor The single common variance or factor that is common to (i.e., empirically intercorrelates with) different intelligence tests (general).
A substance required for the growth of a specific organism.
(05 Mar 2000)
Castle's intrinsic factor A mucoprotein normally secreted by the epithelium of the stomach and that binds vitamin B12, the intrinsic factor/B12 complex is selectively absorbed by the distal ileum, though only the vitamin is taken into the cell.
(18 Nov 1997)
maturation factor <biochemistry> Member of the water soluble B vitamin group, important in the proper function of the nervous system and important in proper carbohydrate, protein and fat metabolism.
(27 Sep 1997)
maturation-promoting factor <enzyme> A protein kinase that drives both the mitotic and meiotic cycles in all eukaryotic organisms.
In meiosis it induces immature oocytes to undergo meiotic maturation. In mitosis it has a role in the G2/M phase transition. Once activated by cyclins, maturation-promoting factor directly phosphorylates some of the proteins involved in nuclear envelope breakdown, chromosome condensation, spindle assembly, and the degradation of cyclins.
The catalytic subunit of maturation-promoting factor is protein p34cdc2.
Acronym: MPF
(12 Dec 1998)
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