| ¿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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| ARMS | adverse reaction monitoring system; amplification refractory mutation system |
|---|---|
| FACL | fatty acid coenzyme ligase |
| GLUL | glutamate (ammonia) ligase |
| LR | labeled release; laboratory references; laboratory report; labor room; lactated Ringer [solution]; l... |
| amp | ampere; amplification; ampule; amputation, amputee |
| LCR | Ligase Chain Reaction |
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| 4CL | 4-Coumarate:coenzyme A ligase |
| RT-PCR | Reverse transcriptase-polymerase chain reaction amplification |
| 'RACE' | 3' rapid amplification of cDNA ends |
| 3' RACE | 3' rapid amplification of cDNA ends |
| ligase amplification reaction | <molecular biology> Method for detecting small quantities of a target DNA, with utility similar to PCR. It relies on DNA ligase to join adjacent synthetic oligonucleotides after they have bound the target DNA. Their small size means that they are destabilised by single base mismatches and so form a sensitive test for the presence of mutations in the target sequence. (18 Nov 1997) |
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| amplification | <molecular biology> An increase in the number of copies of a specific DNA fragment, can be in vivo or in vitro. See: cloning, polymerase chain reaction. (09 Oct 1997) |
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| random amplification of polymorphic DNA | <molecular biology> A term originally invented by polymer chemists to describe a disordered tangle of a linear polymer chain with curved sections. In DNA parlance the random coil refers to the structure that results from melting or other forms of separation of the double helix, i.e. Helix coil transition. (18 Nov 1997) |
| gene amplification | <molecular biology> Selective replication of DNA sequence within a cell, producing multiple extra copies of that sequence. The best known example occurs during the maturation of the oocyte of Xenopus, where the set (normally 500 copies) of ribosomal RNA genes is replicated some 4,000 times to give about 2 million copies. (18 Nov 1997) |
| genetic amplification | A process for producing an increase in pertinent genetic material, particularly for increasing the proportion of plasmid DNA to that of bacterial DNA. Includes the production of extrachromosomal copies of the genes for RNA. (05 Mar 2000) |
| DNA amplification | <molecular biology> The use of enzymes in making millions or billions of copies of a single DNA sequence (see PCR). (14 Nov 1997) |
| acetate-CoA ligase | <enzyme> An enzyme that catalyses the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. Chemical name: Acetate:CoA ligase (AMP-forming) Registry number: EC 6.2.1.1 (12 Dec 1998) |
| acetyl-CoA ligase | A ligase that catalyses the reaction of acetate and CoA and ATP to form AMP, pyrophosphate, and acetyl-CoA. A key step in the activation of acetate. Synonym: acetate thiokinase, acetate-CoA ligase, acetyl-activating enzyme, acetyl-CoA synthetase. (05 Mar 2000) |
| alanine-trna ligase | <enzyme> An enzyme that activates alanine with its specific transfer RNA. Chemical name: L-Alanine:tRNA(Ala) ligase (AMP-forming) Registry number: EC 6.1.1.7 (12 Dec 1998) |
| alanyl-seryl ligase | <enzyme> Catalyses incorporation of terminal ala-ser to peptidoglycan; associated with vancomycin resistance; isolated from enterococcus casseliflavus Registry number: EC 6.3.2.- Synonym: alanylseryl ligase, d-alanyl-d-seryl ligase, d-alanylseryl ligase, ala-ser ligase, vanc ligase, vanc2 protein (26 Jun 1999) |
| arginine-trna ligase | <enzyme> An enzyme that activates arginine with its specific transfer RNA. Chemical name: L-Arginine:tRNA(Arg)ligase (AMP-forming) Registry number: EC 6.1.1.19 (12 Dec 1998) |
| aspartate-ammonia ligase | <enzyme> An enzyme that catalyses the formation of asparagine from ammonia and aspartic acid, in the presence of ATP. Chemical name: L-Aspartate:ammonia ligase (AMP-forming) Registry number: EC 6.3.1.1 (12 Dec 1998) |
| aspartate-trna ligase | <enzyme> An enzyme that activates aspartic acid with its specific transfer RNA. Chemical name: L-Aspartate:tRNA-(Asp) ligase (AMP-forming) Registry number: EC 6.1.1.12 (12 Dec 1998) |
| benzoate coenzyme A ligase | <enzyme> From rhodopseudomonas palustris; involved in anaerobic degradation of benzoate; high specificity for benzoate and fluorobenzoate Registry number: EC 6.2.1.25 Synonym: benzoate-CoA ligase, benzoic acid coenzyme a ligase, benzoyl-CoA ligase, benzoyl CoA synthetase (26 Jun 1999) |
| bile acid-CoA ligase | <enzyme> Catalyses the synthesis of all bile acid-coas; in order to measure the activity of all bile acids, the bile acid is coupled with c(14)-glycine and measured with bile acid-CoA glycine-taurine n-acetyltransferase Registry number: EC 6.2.1.- (26 Jun 1999) |
| butyrate-CoA ligase | Fatty acid thiokinase (medium chain), a ligase forming acyl-CoA's from medium-chain fatty acids and CoA with the conversion of ATP to AMP and PPi. A key step in activation of fatty acids. Synonym: acyl-activating enzyme, butyryl-CoA synthetase, octanoyl-CoA synthetase. (05 Mar 2000) |
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