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    ÇѱÛ
  • complement fixation
    º¸Ã¼°áÇÕ
  • complement fixation inhibition test
    º¸Ã¼°áÇÕ¾ïÁ¦°Ë»ç
  • complement fixation reaction
    º¸Ã¼°áÇÕ¹ÝÀÀ
  • complement fixation test
    º¸Ã¼°áÇÕ°Ë»ç
  • complement inhibitor
    º¸Ã¼¾ïÁ¦Á¦, µµ¿òü¾ïÁ¦Á¦
  • complement mediated lysis
    º¸Ã¼¸Å°³¿ëÇØ, µµ¿òü¸Å°³¿ëÇØ
  • complement profile
    º¸Ã¼Ãø¸é»ó
  • complement receptor
    º¸Ã¼¼ö¿ëü
  • complement system
    º¸Ã¼°è, µµ¿òü°èÅë
  • complement-dependent cytotoxicity
    º¸Ã¼ÀÇÁ¸¼¼Æ÷µ¶¼º
  • complement-fixing antibody
    º¸Ã¼°áÇÕÇ×ü, µµ¿òü°áÇÕÇ×ü
  • complement-induced
    º¸Ã¼À¯µµ-
  • complement-mediated
    º¸Ã¼¸Å°³-
  • complement-mediated cytotoxicity
    º¸Ã¼¸Å°³¼¼Æ÷µ¶¼º
  • dominant complement
    ¿ì¼ºº¸Ã¼
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  • complement-mediated
    µµ¿òü¸Å°³-
  • classic complement pathway
    º¸Ã¼ÀüÇüÀû°æ·Î, µµ¿òüÀüÇüÀû°æ·Î
  • complement cascade
    º¸Ã¼¿¬¼âÁõÆø¹ÝÀÀ
  • complement component
    µµ¿òü¼ººÐ
  • complement deficiency
    µµ¿òü°áÇÌ
  • complement fixation
    µµ¿òü°áÇÕ
  • complement inhibitor
    º¸Ã¼¾ïÁ¦Á¦, µµ¿òü¾ïÁ¦Á¦
  • complement profile
    µµ¿òÃ¼Ãø¸é»ó
  • complement receptor
    µµ¿òü¼ö¿ëü, º¸Ã¼¼ö¿ëü
  • complement splitting
    µµ¿òüºÐ¿­, º¸Ã¼ºÐ¿­
  • complement system
    µµ¿òü°èÅë, º¸Ã¼°èÅë
  • complement typing
    º¸Ã¼Çüº°°Ë»ç
  • complement deficient state
    µµ¿òü°áÇÌ»óÅÂ, º¸Ã¼°áÇÌ»óÅÂ
  • complement fixation reaction
    º¸Ã¼°áÇÕ¹ÝÀÀ, µµ¿òü°áÇÕ¹ÝÀÀ
  • complement fixation test
    µµ¿òü°áÇÕ½ÃÇè, º¸Ã¼°áÇÕ½ÃÇè
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    ÇѱÛ
  • activation energy
    Ȱ¼ºÈ­¿¡³ÊÁö
  • activation gate
    °³¹æ °ü¹®(ËÒÛÁμڦ)
  • activation process
    Ȱ¼ºÈ­°úÁ¤.
  • activation, polyclonal
    ´Ù¼¼Æ÷±ºÈ°¼º, ¿©·¯¹«¸®È°¼º
  • activation, polyclonal B cell
    ´Ù¼¼Æ÷±º B¼¼Æ÷Ȱ¼º, ¿©·¯¹«¸® B¼¼Æ÷Ȱ¼º
  • heat of activation
    Ȱ¼ºÈ­¿­(üÀàõûýæð)
  • photochemical activation
    ±¤È°¼ºÈ­(Ë´Ì· ËÛÌ´).
  • plasmin activation inhibitor
    Çö󽺹ÎȰ¼ºÈ­¾ïÁ¦Á¦(¡­üÀàõûùåäð¤ð¥)
  • polyclonal B cell activation
    B¼¼Æ÷ ´Ù(¼ö)Ŭ·ÐȰ¼º, B¼¼Æ÷ ¿©·¯¹«¸®È°¼º
  • polyclonal activation
    ´Ù(¼ö)Ŭ·ÐȰ¼º, ¿©·¯¹«¸®È°¼º
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  • macrophage,activation of
    Ȱ¼ºÈ­(üÀàõûù)
  • neutron activation analysis
    Áß¼ºÀÚ¹æ»çÈ­ºÐ¼®(~Û¯ÞÒûùÝÂà°).
  • photochemical activation
    ±¤È°¼ºÈ­(Ë´Ì· ËÛÌ´).
  • plasmin activation inhibitor
    Çö󽺹ÎȰ¼ºÈ­¾ïÁ¦Á¦(¡­üÀàõûùåäð¤ð¥)
  • polyclonal B cell activation
    B¼¼Æ÷ ´Ù(¼ö)Ŭ·ÐȰ¼º, B¼¼Æ÷ ¿©·¯¹«¸®È°¼º
  • polyclonal activation
    ´Ù(¼ö)Ŭ·ÐȰ¼º, ¿©·¯¹«¸®È°¼º
  • sleep activation
    ¼ö¸éºÎȰ(¹ý)(¡­Ý¥üÀÛö) ³úÆÄ(Òà÷î)ÀÇ .
  • thermal activation
    ¿­È°¼ºÈ­¹ÝÀÀ(æðüÀàõûù Úãëë).
  • tissue plasminogen activation
    Á¶Á÷ ÇöóÁî¹Ì°Õ Ȱ¼º
  • tissue plasminogen activation inhibitor
    Á¶Á÷ ÇöóÁî¹Ì³ë°Õ Ȱ¼º ¾ïÁ¦ÀÎÀÚ
  • trypsinogen activation peptide(TAP)
  • ventricular activation
    ½É½ÇÈïºÐ(ãýãøýéÝÇ).
  • ventricular activation
    ½É½ÇÈïºÐ(ãýãøýéÝÇ)
  • ventricular activation time
    ½É½ÇÈïºÐ½Ã°£(ãýãøýéÝÇãÁÊà).
  • antibody, complement binding
    º¸Ã¼°áÇÕÇ×ü
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  • energy of activation
    Ȱ¼ºÈ­(üÀàõûù) ¿¡³ÊÁö
  • fatty acid activation
    Áö¹æ»ê Ȱ¼ºÈ­ (ò·Û¸ß«üÀàõûù)
  • feed-forward activation
    ¾Õ¸ÔÀÓ È°¼ºÈ­ (üÀàõûù)
  • gene activation
    À¯ÀüÀÚ È°¼ºÈ­(ë¶îîí­üÀàõûù)
  • macrophage activation factor
    ´ë½Ä¼¼Æ÷Ȱ¼ºÀÎÀÚ(ÓÞãÝá¬øàüÀàõì×í­)
  • neutron activation alalysis
    Áß¼ºÀÚ ¹æ»çÈ­ºÐ¼®(ñéàõí­Û¯ÞÒûùÝÂà°)
  • reciprocal activation
    »óº¸ Ȱ¼ºÈ­(ßÓÜÍüÀàõûù)
  • upstream activation sites
    À­ÂÊ È°¼ºÈ­(üÀàõûù)ÀÚ¸®
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AE above-elbow [amputation]; acrodermatitis enteropathica; activation energy; adult erythrocyte; advers...
ARAM antigen recognition activation motif
HIPA heparin-induced platelet activation
INAA instrumental neutron activation analysis
LAG labiogingival; leukocyte antigen group; linguo-axiogingival; lymphangiogram; lymphocyte activation g...
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ARI activation recovery interval
AT Activation time
Ea Energy of activation
FAP Fibroblast Activation Protein
HIPA Heparin-induced platelet activation
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    ¼³¸í
  • serum complement titer
    Ç÷û º¸Ã¼ °¡ÃøÁ¤
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  • sympathetic activation
    ±³°¨½Å°æ°è Ȱ¼º
  • treponema pallidum complement fixation test
    Æ®·¹Æ÷³×¸¶ º¸Ã¼ °áÇÕ ½ÃÇè
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energy of activation Energy that must be added to that already possessed by a molecule or molecules in order to initiate a reaction; usually expressed in the Arrhenius equation relating a rate constant to absolute temperature.
(05 Mar 2000)
enzyme activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1) activation by ions (activators); 2) activation by cofactors (coenzymes); and 3) conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
(12 Dec 1998)
juxtacrine activation Activation of target cells by membrane anchored growth factors, also used for activation of leucocytes by PAF bound to endothelial cell surface.
(18 Nov 1997)
feedback activation The activation of an enzyme by an end product of a biochemical pathway in which that enzyme plays a part. For example, the activation of factors VIII and V by thrombin during blood clotting.
(05 Mar 2000)
feed-forward activation The activation of an enzyme by a precursor of the substrate of that enzyme.
(05 Mar 2000)
upstream activation site A DNA sequence that regulates transcription like an enhancer but does notwork if its located downstream from a promoter.
(09 Oct 1997)
low-activation materials <radiobiology> In fission reactors, one is forced to deal with the radioactive byproducts of the fission process, but in fusion reactors one generally has a choice of what materials to expose to neutrons produced by the fusion process. A major problem for fusion reactors is developing materials (such as for the reactor vacuum vessel structure) which can be exposed to high levels of neutron bombardment without becoming permanently radioactive. Candidate structural materials which have relatively low induced radiactivation (generally relative to stainless steel) are known as low-activation materials, these include titanium, vanadium, and silicon-carbide.
(09 Oct 1997)
lymphocyte activation <haematology> The change in morphology and behaviour of lymphocytes exposed to a mitogen or to an antigen to which they have been primed. The result is the production of lymphoblasts, cells that are actively engaged in protein synthesis and that divide to form effector populations. Should not be confused with transformation of the type associated with oncogenic viruses and activation is therefore perhaps a better term.
(18 Nov 1997)
male chromosome complement The large majority of males have a 46, xy chromosome complement (46 chromosomes including an x and a y chromosome). A minority of males have other chromosome constitutions such as 47,xxy (47 chromosomes including two x chromosomes and a y chromosome) and 47,xyy (47 chromosomes including an x and two y chromosomes).
(12 Dec 1998)
genetic complement <biology, genetics> The set of chromosomes contained within any one particular cell.
(07 May 1998)
receptors, complement Molecules on the surface of some B-lymphocytes and macrophages, that recognise and combine with the c3b, c3d, c1q, and c4b components of complement.
(12 Dec 1998)
receptors, complement 3b Molecular sites on or in some B-lymphocytes and macrophages that recognise and combine with complement 3b. The primary structure of these receptors reveal that they contain transmembrane and cytoplasmic domains, with their extracellular portion composed entirely of thirty short consensus repeats each having 60 to 70 amino acids.
(12 Dec 1998)
receptors, complement 3d Molecular sites on or in B-lymphocytes, follicular dendritic cells, lymphoid cells, and epithelial cells that recognise and combine with complement 3d. Human cr2 serves as a receptor for both c3dg and the gp350/220 glycoprotein of herpes virus 4, human, and binds the monoclonal antibody okb7, which blocks binding of both ligands to the receptor.
(12 Dec 1998)
chromosome complement The whole set of chromosomes for the species. In humans, the chromosome complement (which is also called the karyotype) consists of 46 chromosomes.
(12 Dec 1998)
complement <immunology> A term originally used to refer to the heat labile factor in serum that causes immune cytolysis, the lysis of antibody coated cells and now referring to the entire functionally related system comprising at least 20 distinct serum proteins that is the effector not only of immune cytolysis but also of other biologic functions.
Complement activation occurs by two different sequences, the classic and alternative pathways. The proteins of the classic pathway are termed components of complement and are designated by the symbols C1 through C9.
C1 is a calcium dependent complex of three distinct proteins C1q, C1r and C1s. The proteins of the alternative pathway (collectively referred to as the properdin system) and complement regulatory proteins are known by semisystematic or trivial names. Fragments resulting from proteolytic cleavage of complement proteins are designated with lower case letter suffixes, for example, C3a. Inactivated fragments may be designated with the suffix i, for example C3bi. Activated components or complexes with biological activity are designated by a bar over the symbol for example C1 or C4b, 2a.
The classic pathway is activated by the binding of C1 to classic pathway activators, primarily antigen-antibody complexes containing IgM, IgG1, IgG3, C1q binds to a single IgM molecule or two adjacent IgG molecules.
The alternative pathway can be activated by IgA immune complexes and also by nonimmunologic materials including bacterial endotoxins, microbial polysaccharides and cell walls. Activation of the classic pathway triggers an enzymatic cascade involving C1, C4, C2 and C3, activation of the alternative pathway triggers a cascade involving C3 and factors B, D and P. Both result in the cleavage of C5 and the formation of the membrane attack complex.
Complement activation also results in the formation of many biologically active complement fragments that act as anaphylatoxins, opsonins or chemotactic factors.
(05 Jan 1998)
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