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  • ¿µ¹®
    ÇѱÛ
  • iron binding protein
    ö°áÇմܹéÁú
  • iron-binding capacity
    ö°áÇÕ´É
  • ligand binding site
    ¸®°£µå°áÇÕºÎÀ§
  • olfactory binding protein
    Èİ¢°áÇմܹéÁú
  • orthodontic binding wire
    ±³Á¤¿ë¹­±âö»ç, ±³Á¤¿ë°áÂû¼±
  • protein binding
    ´Ü¹éÁú°áÇÕ
  • sex hormone-binding globulin
    ¼ºÈ£¸£¸ó°áÇձ۷κҸ°
  • antigen receptor
    Ç׿ø¼ö¿ëü
  • adrenergic receptor
    ¾Æµå·¹³¯¸°¼ö¿ëü
  • androgen receptor
    ¾Èµå·Î°Õ¼ö¿ëü
  • beta-adrenergic receptor kinase
    º£Å¸¾Æµå·¹³¯¸°¼ö¿ëüÀλêÈ­È¿¼Ò
  • cold receptor
    ³Ã°¢¼ö¿ë±â
  • complement receptor
    º¸Ã¼¼ö¿ëü
  • corpuscular receptor
    ¼Òü¼ö¿ëü
  • cell surface receptor
    ¼¼Æ÷Ç¥¸é¼ö¿ëü
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  • ¿µ¹®
    ÇѱÛ
  • gonadal steroid-binding globulin
    »ý½Ä»ù½ºÅ×·ÎÀ̵å°áÇձ۷κҸ°
  • sex hormone-binding globulin
    ¼ºÈ£¸£¸ó°áÇÕ±Û·Îºí¸°
  • testosterone-binding globulin
    Å×½ºÅ佺Å׷аáÇձ۷κҸ°
  • thyroxine-binding globulin
    Ƽ·Ï½Å°áÇÕ±Û·Îºí¸°
  • iron binding protein
    ö°áÇմܹéÁú
  • olfactory binding protein
    Èİ¢°áÇմܹé
  • orthodontic binding wire
    ±³Á¤¿ë¹­±âö»ç, ±³Á¤¿ë°áÂû¼±
  • adrenergic receptor
    ¾Æµå·¹³¯¸°¼ö¿ëü
  • androgen receptor
    ¾Èµå·Î°Õ¼ö¿ëü
  • antigen receptor
    Ç׿ø¼ö¿ëü
  • receptor autoradiography
    ¼ö¿ëüÀÚ°¡¹æ»ç¼±¼ú
  • beta-adrenergic receptor kinase
    º£Å¸¾Æµå·¹³¯¸°¼º¼ö¿ëüÀλêÈ­È¿¼Ò
  • receptor blocker
    ¼ö¿ëüÂ÷´ÜÁ¦
  • cell surface receptor
    ¼¼Æ÷Ç¥¸é¼ö¿ëü
  • cholinergic receptor
    Äݸ°¼ö¿ëü
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  • ¿µ¹®
    ÇѱÛ
  • antibody, complement binding
    º¸Ã¼°áÇÕÇ×ü
  • antigen binding capacity
    Ç׿ø°áÇÕ´É(¡­Ì¿ùêÒö).
  • antigen binding fragment
    Ç׿ø°áÇÕºÎÀ§
  • antigen binding site
    Ç׿ø°áÇÕºÎÀ§
  • human zona binding assay
    »ç¶÷Á¤ÀÚ Åõ¸í´ëºÎÂø°Ë»ç
  • plasma protein binding
    Ç÷Àå´Ü¹é°áÇÕ.
  • protein,actin-binding
    ¾×ƾ-°áÇÕ(´Ü¹é)
  • A1 receptor
    A1 ¼ö¿ëü(¼ö¿ë±â, °¨¼ö±â)
  • A2 receptor
    A2 ¼ö¿ëü(¼ö¿ë±â, °¨¼ö±â)
  • CR1 => complement receptor 1
    º¸Ã¼¼ö¿ëü 1
  • CR2 => complement receptor 2
    º¸Ã¼¼ö¿ëü 2
  • CR3 => complement receptor 3
    º¸Ã¼¼ö¿ëü 3
  • CR4 => complement receptor 4
    º¸Ã¼¼ö¿ëü 4
  • Gustatory receptor
    ¹Ì°¢¼ö¿ëü(Ú«ÊÆâ¥é»ô÷)
  • H2 receptor antagonist
    H2 ¼ö¿ëü ±æÇ×Á¦µé
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  • ¿µ¹®
    ÇѱÛ
  • binding energy
    °áÇÕ¿¡³ÊÁö
  • binding energy
    °áÇÕ(Ì¿ùê)¿¡³ÊÁö
  • binding orbit
    °áÇձ˵µ(Ì¿ùêÏùÔ³).
  • binding site
    °áÇÕºÎÀ§.
  • binding site
    °á ÇÕºÎÀ§.
  • calcium-binding protein
    Ä®½· °áÇմܹé(Ì¿ùêÓ±ÛÜ)
  • cap binding protein
    ĸ°áÇմܹéÁú
  • cellular retinol-binding protein
    ¼¼Æ÷³» ·¹Æ¼³î °áÇմܹé
  • competitive protein binding radioassay
    °æÇÕÀû ´Ü¹é°áÇÕ¹æ»çºÐ¼®(¹ý)(¡­Ó±ÛÜ Ì¿ùêÛ¯ÞÒÝÂà°Ûö).
  • complement binding antibody
    º¸Ã¼°áÇÕÇ×ü(ÜÍô÷Ì¿ùêù÷ô÷).
  • corticosteroid binding globulin =CSG
    ÄÚ¸£Æ¼ÄÚ½ºÅ×·ÎÀ̵å°áÇÕ ±Û·ÎºÒ ¸°.
  • cortisol binding globulin
    ÄÚ¸£Æ¼¼Ö°áÇÕ±Û·Îºí¸°.
  • cortisol-binding globulin=transcortin
    ÄÚ¸£Æ¼¼Ö°áÇձ۷κҸ°=Æ®¶õ½ºÄÚ¸£Æ¾
  • cross binding
    ±³Â÷¿¬°á(±³Â÷¿¬°á).
  • human zona binding assay
    »ç¶÷Á¤ÀÚ Åõ¸í´ëºÎÂø°Ë»ç
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  • ¿µ¹®
    ÇѱÛ
  • mineralocorticoid receptor
    ±¤Áú(ÎÎòõ) ÄÚ¸£Æ¼ÄÚÀÌµå ¼ö¿ëü(áôé»ô÷)
  • mobile receptor model
    À̵¿¼ö¿ëü(ì¹ÔÑáôé»ô÷) ¸ðµ¨
  • muscarinic receptor
    ¹«½ºÄ«¸°¼ö¿ëü(áôéÄô÷)
  • nicotinic receptor
    ´ÏÄÚÆ¾¼ö¿ëü(â¥é»ô÷)
  • opiate receptor
    ¾ÆÆíÁ¦(ð¥) ¼ö¿ëü(áôé»ô÷)
  • opioid receptor
    ¾ÆÆí°è(ͧ) ¾à¹°¼ö¿ëü(å·Úªáôé»ô÷)
  • receptor
    ¼ö¿ëü(áôé»ô÷)
  • receptor destroying enzyme
    ¼ö¿ëü ÆÄ±«È¿¼Ò(áôé»ô÷÷òÎÕý£áÈ)
  • receptor down regulation
    ¼ö¿ëü ÇÏÇâ Á¶Àý(áôé»ô÷ù»ú¾ðàï½)
  • receptor element
    ¼ö¿ëü Á¶Àý ¿ä¼Ò(áôé»ô÷ðàï½é©áÈ)
  • receptor gradient
    ¼ö¿ëü ±¸¹è(áôé»ô÷ÎþÛÕ)
  • receptor internalization
    ¼ö¿ëü ³»ÀÔ(áôé»ô÷Ò®ìý)
  • receptor-mediated endocytosis
    ¼ö¿ëü¸Å°³ ¼¼Æ÷³» ÀÌÀÔ(áôé»ô÷ØÚË¿á¬øàÒ®ì¹ìý)
  • ribosome receptor
    ¶óÀ̺¸¼Ø ¼ö¿ëü(áôé»ô÷)
  • spare receptor
    ¿¹ºñ(çãÝá) ¼ö¿ëü (â¥é»ô÷)
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CBG capillary blood gases; coronary bypass graft; corticosteroid-binding globulin; cortisol-binding glob...
FABP fatty acid-binding protein; folate-binding protein
IBC Institutional Biosafety Committee; iodine-binding capacity; iron-binding capacity; isobutyl cyanoacr...
IBP insulin-like growth factor binding protein; International Biological Program; intra-aortic balloon p...
MBP major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
alpha 2MR/LRP alpha (2)-macroglobulin receptor/low density lipoprotein receptor-related protein
ORL1 opioid receptor like receptor
125I 1) inhibited binding of
SREBP 1/sterol regulatory element binding protein
CBF 2/core binding factor
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 5-HT1 receptor antagonist
    5-HT1 ¼ö¿ë±â ±æÇ×Á¦
    ÀÏÂïÀÌ 5-hydroxytry
  • A1 receptor
    A1 ¼ö¿ëü, A1 ¼ö¿ë±â, A1 °¨¼ö±â
  • acetylcholine receptor
    ¾Æ¼¼Æ¿Äݸ° ¼ö¿ëü
  • alpha-adrenergic receptor
    ¾ËÆÄ-¾Æµå·¹³¯¸° ¼ö¿ëü
  • antigen receptor
    Ç׿ø ¼ö¿ëü
  • beta receptor blocker
    º£Å¸ ¼ö¿ëü Â÷´ÜÁ¦
  • C3 receptor
    C3 ¼ö¿ëü
    Ç÷¾× ¼ÓÀÇ ¿©·¯ ¼¼Æ÷¿¡´Â º¸Ã¼ Á¦ 3¼ººÐ¿¡ ´ëÇÑ ¼ö¿ëü¸¦ °¡Áö°í ÀÖ´Â °ÍÀÌ ÀÖ´Ù. B ¸²ÇÁ±¸´Â C3b ¹× C3dÀÇ ¼ö¿ëü¸¦ °¡Áö°í ÀÖ´Ù. T ¸²ÇÁ±¸´Â C3b ¼ö¿ëü´Â À̹ۿ¡ È£Áß±¸, macro
  • deep receptor
    ½ÉºÎ ¼ö¿ëü
  • distance receptor
    °Å¸® ¼ö¿ë±â
  • dominant receptor
    ¿ì¼º ¼ö¿ëü
  • dopamine receptor
    µµÆÄ¹Î ¼ö¿ëü
  • down-regulation of receptor
    ¼ö¿ëü ÇÏÇâ Á¶Àý
  • drug receptor
    ¾à¹° ¼ö¿ëü
  • estrogen receptor protein
    ¿¡½ºÆ®·Î°Õ ¼ö¿ëü ´Ü¹éÁú
  • Fc receptor
    Fc ¼ö¿ëü
    Ç×üÀÇ Fc ºÐÀý°ú °áÇÕÇÏ´Â ¼¼Æ÷ Ç¥¸é ¼ö¿ëüÀ̸ç B ¼¼Æ÷, macro
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cellular retinoic acid binding protein <protein> A cytoplasmic fatty acid binding protein that acts as an initial receptor for the putative morphogen, retinoic acid.
(18 Nov 1997)
retinol-binding protein <molecular biology> Proteins which bind with retinol.
The retinol-binding protein found in plasma has an alpha-1 mobility on electrophoresis and a molecular weight of 21,000-22,000. The protein has one binding site for retinol and is responsible for the transport of vitamin A.
The retinol- protein complex (molecular weight 80,000 to 90,000) circulates in plasma in the form of a protein-protein complex with prealbumin. The retinol-binding protein found in tissue has a molecular weight of 14,000 and carries retinol as a non-covalently-bound ligand.
(03 Jul 1999)
gonadal steroid-binding globulin A protein that transports 65% of the testosterone in plasma.
Synonym: sex steroid-binding globulin.
(05 Mar 2000)
periplasmic binding proteins Transport proteins located within the periplasmic space. Some act as receptors for bacterial chemotaxis, interacting with MCPs. Their mode of action is unclear.
(18 Nov 1997)
ribose binding protein <protein> Periplasmic binding proteins of bacteria that interact either with the ribose transport system or with the methyl accepting chemotaxis protein MCP III (trg).
(18 Nov 1997)
ribosome binding site The region of a messenger RNA molecule that binds the ribosome to initiate translation.
(09 Oct 1997)
GTP-binding protein <molecular biology, protein> There are two main classes of G-proteins, the heterotrimeric G proteins that associate with receptors of the seven transmembrane domain superfamily and are involved in signal transduction and the small cytoplasmic G-proteins.
Regulatory proteins found in all cells. They are versatile molecular switches, involved in the control of a wide range of biological processes - protein synthesis, signal transduction pathways, growth and differentiation. They all act through a common molecular mechanism based on their ability to bind the guanine nucleotides GTP and GDP selectively and with high affinity.
Stimulatory G-proteins are permanently activated by cholera toxin, inhibitory ones by pertussis toxin. Transducin was one of the first of the heterotrimeric G-proteins to be identified.
The small G-proteins are a diverse group of monomeric GTPases that include ras, rab, rac and rho and that play an important part in regulating many intracellular processes including cytoskeletal organisation and secretion. Their GTPase activity is regulated by activators (GAPs) and inhibitors (GIPs) that determine the duration of the active state.
(12 Jul 2000)
RNA-binding proteins Proteins which bind to RNA molecules. Certain structure motifs are common to several of the proteins, such as arginine (arg)-rich tracts, typically consisting of alternating arg-asp, arg-ser, or arg-gly residues. These proteins also tend to have a common ribonucleotide sequence domain.
(12 Dec 1998)
guanosine triphosphate binding protein <protein> A type of protein embedded in the cytoplasmic membrane of the cell which transmits signals from outside the cell (such as from hormones binding to receptors on the outside of the cell) to the inside of the cell, where it causes some sort of biochemical reaction within the cell to the signal (such as the altering of metabolic pathways or gene expression). The process by which the protein does this is unclear but involves exchanging a molecule of GDP for a molecule of GTP.
(09 Oct 1997)
placental calcium-binding protein <protein> Calcium binding protein of placenta, uterus and vasculature containing the EF hand motif.
(18 Nov 1997)
competitive binding assay General term for an assay in which a binder competes for labelled versus unlabelled ligand; following separation of free and bound ligand, the ligand (the analyte assayed) is quantitated by relating bound and unbound ratios to known standards.
See: enzyme-linked immunosorbent assay, radioreceptor assay, immunoassay, enzyme-multiplied immunoassay technique, radioimmunoassay.
Synonym: displacement analysis, saturation analysis.
(05 Mar 2000)
complement binding assay A test for the detection of immune complexes.
(05 Mar 2000)
Con A binding site <biochemistry> A common misuse of the term receptor. Con A binds to the mannose residues of many different glycoproteins and glycolipids and the binding is therefore not to a specific site.
It could be argued that the receptor is the Con A and cells have Con A ligands on their surfaces: certainly this would be less confusing.
(05 Jan 1998)
corticosteroid-binding globulin <chemical> Chemical name: Transcortins
(12 Dec 1998)
corticosteroid-binding protein <chemical> Chemical name: Transcortins
(12 Dec 1998)
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