| ¿µ¹® | immunological reaction | ÇÑ±Û | ¸é¿ª¹ÝÀÀ |
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| ¼³¸í | »ýüÀÇ ¸ö ¾È¿¡¼ »ý±ä ¹°ÁúÀ̳ª ¸ö ¹Û¿¡¼ µé¾î¿Â ¹°ÁúÀÌ »ýü¿Í ´Ù¸¦ ¶§ ÀÚ±â ü³»ÀÇ ÅëÀϼº°ú °³Ã¼ÀÇ »ýÁ¸ À¯Áö ¹× Á¾ÀÇ Á¸¼ÓÀ» À§ÇÏ¿© ±× ¹°ÁúµéÀ» Á¦°ÅÇÏ´Â ÀÏ·ÃÀÇ »ýü ¹ÝÀÀ. ´Ù½Ã ¸»ÇØ B¼¼Æ÷¿¡ ÀÇÇÑ Ç×ü»ý»ê, T¼¼Æ÷¸¦ Áß½ÉÀ¸·Î ÇÏ´Â ¼¼Æ÷¼º ¸é¿ª, ¸é¿ª°ü¿ë, ¸é¿ª±â¾ï µîÀÇ »ýü ³» ¹ÝÀÀÀ» ¸»ÇÑ´Ù. Å«Æ÷½Ä¼¼Æ÷´Â Ç׿øÀ» ó¸®Çؼ ƯÀÌÀûÀÎ Ç׿ø°áÁ¤±â¸¦ °®´Â ºÐÀÚ·Î ¹Ù²ã, Ç׿ø°ú ÁÖ¿äÁ¶Á÷ ÀûÇÕÀ¯ÀüÀÚº¹ÇÕü¸¦ ¼¼Æ÷Ç¥¸é¿¡ Ç¥ÇöÇϸç, T¼¼Æ÷·Î Àü´ÞÇÑ´Ù. ÇÑÆí B¼¼Æ÷´Â Å«Æ÷½Ä¼¼Æ÷ ³»¿¡¼ ó¸®µÈ Ç׿øÀÇ °áÁ¤±â¸¦ ÀνÄÇÏ¿© ´ëÀÀÇϴ ƯÀÌÀûÇ×ü¸¦ »ý»êÇÏ¿© Ç׿øÀ» ó¸®ÇÑ´Ù. |
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| ¿µ¹® | reaction formation | ÇÑ±Û | ¹Ýµ¿Çü¼º, ¹ÝÀÀÇü¼º |
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| ¼³¸í | ¾ï¾Ðº¸´Ù ´õ Àû±ØÀûÀÎ ¹æ¾î¸ÞÄ¿´ÏÁòÀ̸ç, ¹«ÀǽÄÀûÀÎ »ý°¢, ¼Ò¿ø, Ãæµ¿ÀÌ ³Ê¹«³ªµµ ¹Þ¾Æµé¿©Áú ¼ö ¾ø´Â °ÍÀÏ °æ¿ì¿¡ À̿ʹ Á¤¹Ý´ë ¹æÇâÀÇ °ÍÀ» °Á¶ÇÔÀ¸·Î½á ±×·± ¹«ÀǽÄÀûÀÎ °ÍµéÀÌ ÀǽĵÇÁö ¾Ê°Ô ÇÏ´Â °úÁ¤. ¿¹¸¦ µé¸é °¡Àå °¡ÇÐÀûÀÎ ¼º°ÝÀÇ »ç¶÷ÀÌ »ýÃ¼ÇØºÎ ¹Ý´ë·ÐÀÚ°¡ µÇ´Â °æ¿ì¸¦ µé ¼ö ÀÖ´Ù. À̰ÍÀº ¶Ç °¡½¿ ±íÀÌ Àá°ÜÀÖ´Â µÎ·Á¿òÀÌ ÀǽĵǴ °ÍÀ» ÇÇÇϱâ À§Çؼ µÎ·Á¿òÀÇ ´ë»óÀÌ µÇ´Â Çൿ¿¡ °ñ¸ôÇÏ´Â °æ¿ìµµ Æ÷ÇÔÀÌ µÈ´Ù. ¿¹¸¦ µé¸é, ³²ÀÚ¿¡°Ô »óó¹ÞÁö ¾ÊÀ»±î ÇÏ´Â µÎ·Á¿ò¿¡ °¡µæ Âù ¼Ò³à°¡ ÀÌ °°Àº µÎ·Á¿òÀ» ºÎÁ¤ÇÏ·Á´Â ¼ö´ÜÀ¸·Î ³ÀâÇÑ ¼ºÇàÀ§¿¡ °ñ¸ôÇÏ´Â °æ¿ì°¡ ÀÖ´Ù. ¶Ç ÀüóÀÇ Àڳฦ ¹Ì¿öÇÏ´Â °è¸ð°¡ ¿ÀÈ÷·Á Áö³ªÄ¥ Á¤µµ·Î ±× ¾ÆÀ̸¦ ±Í¿©¿öÇÏ´Â ÀÏ µûÀ§ÀÌ´Ù. |
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| ¿µ¹® | complement fixation reaction | ÇÑ±Û | º¸Ã¼°áÇÕ ¹ÝÀÀ, µµ¿òü°áÇÕ¹ÝÀÀ |
|---|---|---|---|
| ¼³¸í | Ç×ü¿ÍÀÇ ¹ÝÀÀ¿¡ ÀÖ¾î¼ º¸Ã¼¿Í °áÇÕÇÏ´Â Ç×ü¸¦ °Ë»çÇÏ´Â ¹æ¹ýÀ¸·Î, ÀÌ ¹ÝÀÀÀº ÃÖÃÊ¿¡ ±âÁöÇ׿ø, ÇǰËÇ÷û ¹× º¸Ã¼¸¦ È¥ÇÕÇÑ´Ù. Á¦2´Ü°è¿¡¼´Â ÀûÇ÷±¸¿Í À̰Ϳ¡ ´ëÀÀÇÏ´Â ¿ëÇ÷¼ÒÀÇ È¥ÇÕ¾×À» °¡ÇÑ´Ù. º» ¹ÝÀÀÈÄ ¿ëÇ÷ÀÌ ÀϾÁö ¾ÊÀ¸¸é º»Ã¼´Â Ç׿øÇ×ü°áÇÕ¹°¿¡ °áÇÕÇÑ °ÍÀÌ µÇ¾î ¾ç¼ºÀÌ µÇÁö¸¸, ¿ëÇ÷ÀÌ ÀÏ¾î³ °æ¿ì º¸Ã¼´Â °áÇÕÇÏÁö ¾Ê¾Æ ¼ÒºñµÇÁö ¾Ê±â ¶§¹®¿¡ À½¼ºÀÌ µÈ´Ù. º» ¹ÝÀÀÀº ±âÁöÇ÷ûÀ» ½á¼ Ç׿ø°ËÃâ¿¡ ÀÀ¿ëÇÒ ¼ö ÀÖÀ¸¸ç, ¸¶ÀÌÄÚÇö󽺸¶, ¸®ÄÉÃ, Ŭ¶ó¹Ìµð¾Æ, ¹ÙÀÌ·¯½º, ¸Åµ¶ µîÀÇ Áø´Ü¿¡ ¾²ÀδÙ. |
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| ¿µ¹® | transfusion reaction | ÇÑ±Û | ¼öÇ÷ºÎÀÛ¿ë, ¼öÇ÷¹ÝÀÀ |
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| ¼³¸í | ¼öÇ÷ÇÏ¿´À» ¶§¿¡ ȯÀÚ¿¡°Ô ÀϾ´Â ¹ÝÀÀ. ¾Ë·¹¸£±â ¹ÝÀÀ°ú ¿ëÇ÷ ¹ÝÀÀÀÌ ÀÖ´Ù. |
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| ¿µ¹® | graft versus host reaction | ÇÑ±Û | ÀÌ½ÄÆí´ë ¼÷ÁÖ¹ÝÀÀ |
|---|---|---|---|
| ¼³¸í | ¸é¿ªÀ̶õ ÀÚ½ÅÀÇ °Í°ú ÀÚ½ÅÀÇ °ÍÀÌ ¾Æ´Ñ °ÍÀ» ±¸ºÐÇØ¼ ÀÚ½ÅÀÇ °ÍÀÌ ¾Æ´Ñ °ÍÀ» °ø°ÝÇÏ¿© »ý¹°ÇÐÀû Ȱ¼ºÀ» ¾ø¾Ö°Å³ª Á¦°ÅÇÏ´Â °ÍÀÌ´Ù. ÀÌ ¸é¿ªÀº ÁÖ·Î Ç÷¾×¿¡ ÀÖ´Â ¼¼Æ÷¿¡ ÀÇÇØ¼ ÀÌ·ç¾îÁø´Ù. ƯÈ÷ ¸²ÇÁ±¸´Â ÀÌ ¸é¿ª¿¡ ÁßÃßÀûÀÎ ¿ªÇÒÀ» ÇÏ´Â ¼¼Æ÷ÀÌ´Ù. ÀÌ½ÄÆí´ë¼÷ÁÖ¹ÝÀÀÀ̶ó´Â °ÍÀº À̽ĵǾî¿Â Á¶Á÷¿¡ Á¸ÀçÇϴ ŸÀÎÀÇ Ç÷±¸µéÀÌ ¼÷ÁÖÀÇ ¼¼Æ÷¸¦ °ø°ÝÇÏ´Â °ÍÀ» ¸»ÇÑ´Ù. Áï À̽ĵǾî¿Â Á¶Á÷°ú ÇÔ²² µé¾î¿Â Ç÷±¸µéÀÌ À̽ÄÀ» ¹ÞÀº »ç¶÷ÀÇ ¼¼Æ÷¸¦ ŸÀÎÀÇ °ÍÀ¸·Î ÀÎÁöÇØ¼ °ø°ÝÇÏ´Â Çö»óÀÌ´Ù. À̰ÍÀº À̽ÄÀ» ¹ÞÀº »ç¶÷ÀÇ ¸é¿ª»óŰ¡ Á¤»óÀûÀÏ °æ¿ì¿¡´Â ÀϾÁö ¾Ê´Âµ¥ ¿Ö³ÄÇÏ¸é ¸é¿ª»óŰ¡ Á¤»óÀÏ °æ¿ì¿¡´Â À̽ĵǾî¿Â Àå±â¿Í ´õºÒ¾î µé¾î¿Â ŸÀÎÀÇ Ç÷±¸µéÀ» À̽ÄÀ» ¹ÞÀº »ç¶÷ÀÇ Ç÷±¸°¡ ŸÀÎÀÇ °ÍÀ¸·Î ÀÎÁöÇØ¼ °ø°ÝÀ» ÇÏ°í ¼ýÀûÀ¸·Î À¯¸®ÇÏ¿© ¸ðµÎ Á×ÀÏ ¼ö°¡ Àֱ⠶§¹®ÀÌ´Ù. |
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| PAP | pancreatitis-associated protein; Papanicolaou [test]; papaverine; passive-aggressive personality; pa... |
|---|---|
| TPO | thyroid peroxidase; tryptophan peroxidase |
| LR | labeled release; laboratory references; laboratory report; labor room; lactated Ringer [solution]; l... |
| AAR | active avoidance reaction; acute articular rheumatism; antigen-antiglobulin reaction |
| APR | abdominoperineal resection; absolute proximal reabsorption; acute phase reaction or reactant; amebic... |
| PAP | Peroxidase Anti Peroxidase |
|---|---|
| PAP | peroxidase anti peroxidase method |
| PAP | peroxidase anti-peroxidase complex |
| TPO | Anti-thyroid peroxidase |
| APX | Ascorbate peroxidase |
| peroxidase reaction | Formation of indophenol blue by the action of an oxidizing enzyme present in certain cells and tissues when they are treated with a solution of alpha-naphthol and dimethylparaphenylenediamine; by this method, cells of the myelocyte series, which give a positive reaction, may be distinguished from those of the lymphocyte series, which give a negative reaction; endothelial leukocytes give a variable reaction, probably positive when they have phagocytised the debris of myeloid cells. Synonym: Nadi reaction. (05 Mar 2000) |
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| ascorbate peroxidase | <enzyme> Occurs in the stroma as a soluble form (sap28) and also in the thylakoids as membrane-bound form (sap22) in angiosperm chloroplasts Registry number: EC 1.11.1.11 Synonym: ascorbic acid peroxidase, l-ascorbic acid peroxidase, stromal ascorbate peroxidase, thylakoid-bound ascorbate peroxidase (26 Jun 1999) |
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| barley peroxidase | <enzyme> Endosperm specific enzyme; amino acid sequence given in first source Registry number: EC 1.11.1.- Synonym: b peroxidase 1, barley seed-specific peroxidase bp 1, barley seed peroxidase bp 2a (26 Jun 1999) |
| caffeate peroxidase | <enzyme> Catalyses dimerization of ferulic acid or caffeic acid via oxidative coupling and formation of beta,beta-linkage to lignan-type cpds 8,8'-bis(caffeic acid) or 8,8'-bis(ferulic acid) Registry number: EC 1.11.1.- (26 Jun 1999) |
| manganese peroxidase | <enzyme> Haem enzyme from phanerochaete chrysosporium which oxidises mn(ii) to mn(iii) which then directly oxidises a variety of organic substrates including various polymeric dye; mnp2 encodes isozyme 2 Registry number: EC 1.11.1.- Synonym: mn-peroxidase, manganese-dependent peroxidase, mnp2 gene product (26 Jun 1999) |
| glutathione peroxidase | <enzyme> A detoxifying enzyme that eliminates hydrogen peroxide and organic peroxides. Glutathione is an essential cofactor for the enzyme and its reaction involves the oxidation of glutathione (GSH) to glutathione disulphide (GSSG). The GSSG is then reduced to GSH by glutathione reductase. Glutathione peroxidase, (GPX), has a selenocysteine residue in its active site. Three forms of the enzyme exist: cy toplasmic GPX, plasma GPX and phospholipid hydroperoxide GPX. (18 Nov 1997) |
| chloride peroxidase | <enzyme> An enzyme that catalyses the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. Chemical name: Chloride:hydrogen-peroxide oxidoreductase Registry number: EC 1.11.1.10 (12 Dec 1998) |
| peroxidase | <enzyme> A haem enzyme that catalyses reduction of hydrogen peroxide by a substrate that loses two hydrogen atoms. Within cells, may be localised in peroxisomes. Coloured reaction products allow detection of the enzyme with high sensitivity, so peroxidase coupled antibodies are widely used in microscopy and ELISA. Lactoperoxidase is used in the catalytic surface labelling of cells by radioactive iodine. (18 Nov 1997) |
| peroxidase stain | <technique> A method for demonstrating peroxidase granules in some neutrophils and in eosinophils; the enzyme promotes the oxidation of benzidine by hydrogen peroxide; tissues treated with horseradish peroxidase can also have the enzyme detected in the electron microscope. (05 Mar 2000) |
| Rip1 peroxidase | <enzyme> Isolated from rhizobium; do not confuse with rip1 gene product Registry number: EC 1.11.1.- Synonym: rip1 gene product, peroxidase, rhizobium-induced peroxidase rip1 (26 Jun 1999) |
| cholera toxin, B subunit-horseradish peroxidase | <chemical> Conjugate of horseradish peroxidase and cholera toxin Synonym: bhrp, horseradish peroxidase-cholera toxin b subunit, cholera toxin-horseradish peroxidase, horseradish peroxidase-cholera toxin, ib4-hrp (26 Jun 1999) |
| phospholipid-hydroperoxide glutathione peroxidase | <enzyme> Selenoenzyme found in biological materials; different from glutathione peroxidase EC 1.11.1.9 Registry number: EC 1.11.1.- Synonym: pH-gperoxidase (26 Jun 1999) |
| wheat germ agglutinin-horseradish peroxidase conjugate | <chemical> The lectin wheatgerm agglutinin conjugated to the enzyme horseradish peroxidase. It is widely used for tracing neural pathways. Pharmacological action: molecular probes. (12 Dec 1998) |
| wheat peroxidase | <enzyme> Gene of this enzyme is neither pathogen- nor wound-induced in leaves but is constitutively expressed in roots; amino acid sequence given in first source Registry number: EC 1.11.1.- Synonym: triticum peroxidase (26 Jun 1999) |
| porphyrin cytochrome c peroxidase | <enzyme> From yeast; haem group of cytochrome c peroxidase (EC 1.11.1.5) replaced by protoporphyrin ix Registry number: EC 1.11.1.- Synonym: pcc-peroxidase (26 Jun 1999) |
| cytochrome C553 peroxidase | <enzyme> A haem group of cytochrome-c peroxidase (EC 1.11.1.5); catalytically active in both the oxidised and half-reduced states; from nitrosomonas europaea; partial amino acid sequence given in first source Registry number: EC 1.11.1.- (26 Jun 1999) |
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