| ¿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 |
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| 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 |
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| 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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| FACL | fatty acid coenzyme ligase |
|---|---|
| GLUL | glutamate (ammonia) ligase |
| LR | labeled release; laboratory references; laboratory report; labor room; lactated Ringer [solution]; l... |
| HCG, hCG | Human Chorionic Gonadotropin; »ç¶÷À¶¸ð¼º¼º¼±ÀÚ±ØÈ£¸£¸ó 1. Placental Glycoprotein Hormone &nbs... |
| kappa | a light chain of human immunoglobulins [chain] |
| LCR | Ligase Chain Reaction |
|---|---|
| 4CL | 4-Coumarate:coenzyme A ligase |
| AS-PCR | Allele specific polymerase chain reaction |
| AP-PCR | Arbitrarily primed Polymerase Chain Reaction |
| AP PCR | Arbitrary primed polymerase chain reaction |
| xenobiotic medium chain fatty acid - coenzyme A ligase | <enzyme> Partial amino acid sequence of enzyme from bovine liver mitochondria given I first source; has high sequence homology to human and rat sa protein Registry number: EC 6.2.1.- Synonym: xl-i ligase, xl-i carboxylic acid - CoA ligase (26 Jun 1999) |
|---|---|
| long-chain-fatty-acid-(acyl-carrier-protein) ligase | <enzyme> Fatty acid, acyl-carrier-protein-sh and ATP gives acyl-(acyl-carrier-protein), AMP and ppi Registry number: EC 6.2.1.20 Synonym: fatty acid-acyl carrier protein ligase (AMP), acyl-(acyl-carrier-protein)synthetase, aacp synthetase, fatty acyl-acyl carrier protein synthase, vibrio harveyi, acyl-(acyl-carrier-protein) synthetase, acyl-acp synthetase (26 Jun 1999) |
| long-chain-fatty-acid-CoA ligase | <enzyme> Fatty acid thiokinase (long-chain), a ligase forming acyl-CoA, AMP, and pyrophosphate from long-chain fatty acids, ATP, and coenzyme A. Activity is independent of phosphatidylcholine Registry number: EC 6.2.1.3 Synonym: acyl-activating enzyme, dodecanoyl-CoA synthetase, fatty acid thiokinase (long chain), acid-coenzyme a ligase, fatty acid-CoA ligase, acyl-CoA synthetase, acyl-CoA ligase, coash ligase, ciprofibroyl-CoA synthetase, pristanoyl-CoA synthetase, palmityl CoA synthetase, palmitoyl CoA synthetase, palmitoyl CoA ligase, fatty acyl-CoA synthetase, very long chain fatty acid acyl-CoA synthetase, vlcfa acyl-CoA synthetase, nafenopin-CoA ligase, palmitoyl-CoA synthase, faa2 gene product, faa2p protein, vlacs enzyme (26 Jun 1999) |
| chain, orthodontic chain | <dentistry> A stretchable plastic chain used to hold archwires into brackets and to moke teeth. (08 Jan 1998) |
| 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) |
| chain reaction | A reaction in which a product reacts and thus continues the reaction. (09 Oct 1997) |
| polymerase chain reaction | <molecular biology, technique> The first practical system for in vitro amplification of DNA and as such one of the most important recent developments in molecular biology. Two synthetic oligonucleotide primers, which are complementary to two regions of the target DNA (one for each strand) to be amplified, are added to the target DNA (that need not be pure), in the presence of excess deoxynucleotides and Taq polymerase, a heat stable DNA polymerase. In a series (typically 30) of temperature cycles, the target DNA is repeatedly denatured (around 90_C), annealed to the primers (typically at 50-60_C) and a daughter strand extended from the primers (72_C). As the daughter strands themselves act as templates for subsequent cycles, DNA fragments matching both primers are amplified exponentially, rather than linearly. The original DNA need thus be neither pure nor abundant and the polymerase chain reaction has accordingly become widely used not only in research, but in clinical diagnostics and forensic science. Acronym: PCR (14 Oct 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) |
Synonyms : Chain Reaction, Ligase, Chain Reactions, Ligase, Ligase Chain Reactions, Reaction, Ligase Chain, Reactions, Ligase Chain
| ligase chain reaction |
(LCR) A technique for determining the presence or absence of a specific nucleotide pair within a target gene.
Ãâó: www.fao.org/docrep/003/X3910E/X3910E15.htm
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