| ¿µ¹® | serum enzyme | ÇÑ±Û | Ç÷ûȿ¼Ò |
|---|---|---|---|
| ¼³¸í | Ç÷û ³»¿¡ Æ÷ÇԵǾî ÀÖ´Â ¿©·¯ °¡Áö È¿¼Ò¸¦ ÀÏÄ´ ¸»ÀÌ´Ù. |
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| ¿µ¹® | enzyme | ÇÑ±Û | È¿¼Ò |
|---|---|---|---|
| ¼³¸í | »ý¹°Ã¼ ¼¼Æ÷¼Ó¿¡¼ ÇÕ¼ºµÇ°í, ÁÖ·Î ¼¼Æ÷³»¿¡¼ ÁøÇàµÇ´Â ÈÇйÝÀÀÀ» Ã˸ÅÇÏ´Â ´Ü¹éÁú·Î ½ÃÇè°ü³»¿¡¼µµ °°Àº Ã˸ÅÀÛ¿ëÀ» ÇÑ´Ù. ÀÌ È¿¼Ò´Â ÀΰøÀûÀ¸·Î ¸¸µç ¾î¶² Ã˸ÅÁ¦º¸´Ù ±× ƯÀ̼º°ú Ã˸ÅÀÛ¿ëÀÌ Å¹¿ùÇÑ Æ¯º°ÇÑ »ýüºÐÀÚÀÌ´Ù. ½ÅÁø´ë»ç, Áï ¼¼Æ÷³»¿¡¼ ÀϾ´Â ¹°ÁúÀÇ ÈÇÐÀû º¯È¯Àº È¿¼ÒÀÇ ÀÛ¿ë¿¡ ÀÇÇØ ¸Å¿ì ºü¸£°í ¿øÇÒÇÏ°Ô ÀÌ·ç¾îÁø´Ù. À̰ÍÀº È¿¼ÒÀÇ Ã˸ŠȿÀ²ÀÌ ³ôÀº Á¡°ú È¿¼ÒÀÇ ±âÁú ƯÀ̼º ¶§¹®ÀÌ´Ù. È¿¼Ò¹ÝÀÀÀº »ó¿Â, »ó¾Ð, ÃÖÀû pH µî ÀûÀýÇÑ Á¶°Ç ¾Æ·¡¿¡¼ ÁøÇàµÈ´Ù. ¶Ç È¿¼ÒÀÇ ÁÖü°¡ ´Ü¹éÁúÀ̱⠶§¹®¿¡ ´Ü¹éÁúÀ» º¯¼º½ÃŰ´Â ¿, °»ê, °¾ËÄ®¸®, À¯±â¿ë¸Å µî¿¡ ÀÇÇØ ±× ÀÛ¿ëÀ» ÀҴ´Ù. È¿¼Ò´Â »ýü¿¡ ³Î¸® ºÐÆ÷Çϸç, º¹ÀâÇÏ°í ´Ù¾çÇÑ ´ë»ç¹ÝÀÀÀ» Ã˸ÅÇϱ⠶§¹®¿¡ Á¾·ùµµ ¸¹´Ù. ¾Õ¼ ¸»ÇÑ ¹Ù¿Í °°ÀÌ ´ëºÎºÐÀÇ È¿¼Ò´Â ¼¼Æ÷³»¿¡ Á¸ÀçÇÏÁö¸¸, Ç÷¾×°ú ±×¿ÜÀÇ °£Áú¾×¿¡ µé¾î Àֱ⵵ ÇÏ°í ¼ÒÈÈ¿¼Ò·ùó·³ ü¿Ü·Î ºÐºñµÇ´Â °Íµµ ÀÖ´Ù. |
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| ¿µ¹® | enzyme-linked immunoabsorbent assay | ÇÑ±Û | È¿¼Ò¸é¿ªÃøÁ¤¹ý |
|---|---|---|---|
| ¼³¸í | È¿¼Ò°áÇո鿪ÈíÂøÁ¦ °ËÁ¤¹ýÀ¸·Î ¹ø¿ªµÇ°í ÀÖ´Ù. ÀÌ ¹ýÀº Ç׿ø(¶Ç´Â Ç×ü)¿¡ ¾ËÄ®¸® Æ÷½ºÆÄŸ¾ÆÁ¦ ¶Ç´Â Æä¸£¿Á½Ãµð¾ÆÁ¦ µîÀÇ »ê¼Ò¸¦ °áÇÕ½ÃÄÑ µÎ°í ±× »ê¼ÒȰ¼ºÀ» ÁöÇ¥·Î »ï¾Æ Ç׿øÇ×ü¹ÝÀÀÀÇ Á¤µµ¸¦ ¾È ´ÙÀ½ ¿©±â¿¡¼ Ç׿ø(¶Ç´Â Ç×ü)ÀÇ ¾çÀ» ±¸ÇÏ´Â °ÍÀÌ´Ù. ÀÌ ¹ýÀÇ ÀÌÁ¡À¸·Î¼ °í°¨µµ, Á¶ÀÛÀÇ °£´ÜÇÔ ¹× ¹æ»ç¼±¸é¿ªÃøÁ¤¹ýó·³ ¹æ»ç¼º¹°ÁúÀ» »ç¿ëÇÏÁö ¾Ê¾Æµµ µÈ´Ù´Â Á¡À» µé ¼ö ÀÖ´Ù. È£¸£¸óÀ̳ª ¸é¿ª±Û·ÎºÒ¸°ÀÇ Á¤·®¹ýÀ¸·Î¼ ÀÀ¿ë µÇ°í ÀÖÀ¸¸ç ÃøÁ¤¿ë ŰƮµµ ½ÃÆÇµÇ°í ÀÌÀÖ´Ù. |
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| EIA | electroimmunoassay; enzyme immunoassay; enzyme-linked immunosorbent assay; equine infectious anemia;... |
|---|---|
| PACE | Pacing and Clinical Electrophysiology; paired basic amino acid cleaving enzyme; personalized aerobic... |
| ACE | Angiotensin Converting Enzyme = Kininase II = Dipeptidyl Carboxypepti... |
| EIA | 1) Exercise Induced Asthma; ¿îµ¿ À¯¹ß¼º õ½Ä = EIB 2) Enzyme Immu... |
| ELISA | Enzyme-Linked Immuno-Sorbent Assay; È¿¼Ò ¸é¿ª¹ý |
| NP-SH | Non-protein thiol |
|---|---|
| PSH | Plasma thiol |
| PTP | Prohormone thiol protease |
| TMT | Thiol methyltranferase |
| ELISA | Enzyme Linked Immuno Sorbant Assay |
| thiol enzyme | <enzyme> An enzyme whose activity depends on a free thiol group. (05 Mar 2000) |
|---|
| PepC thiol aminopeptidase | <enzyme> A hexameric protein; isolated from lactoccocus lactis; homologous to bleomycin hydrolase; has been sequenced Registry number: EC 3.4.11.- Synonym: thiol aminopeptidase pepc, pepc cysteine aminopeptidase (26 Jun 1999) |
|---|---|
| prohormone thiol protease | <enzyme> Catalyses the final step of (met)enkephalin sythesis in chromaffin granules Registry number: EC 3.4.22.- (26 Jun 1999) |
| O-acetylhomoserine (thiol)-lyase | <enzyme> With hydrogen sulfide, forms homocysteine Registry number: EC 4.2.99.10 Synonym: acetylhomoserine sulfhydrylase, homocysteine synthase, oah sulfhydrylase, o-acetylhomoserine sulfhydrylase, o-acetyl-l-homoserine sulfhydrylase, o-acetylhomoserine-o-acetylserine sulfhydrylase, met25 sulfhydrylase, o-acetylserine-o-acetylhomoserine sulfohydro-lyase, aahshase (26 Jun 1999) |
| O-succinylhomoserine (thiol)-lyase | <enzyme> An enzyme catalyzing the reaction between cystathionine and succinate to form l-cysteine and O-succinyl-l-homoserine. Synonym: cystathionine gamma-synthase. (05 Mar 2000) |
| thiol | 1. The monovalent radical -SH when attached to carbon; a hydrosulfide; a mercaptan. 2. A mixture of sulfurated and sulfonated petroleum oils purified with ammonia; used in the treatment of skin diseases. (05 Mar 2000) |
| thiol activated haemolysins | Cytolytic bacterial exotoxins that act by binding to cholesterol in cell membranes and forming ring like complexes that act as pores. SH groups of these toxins must be in the reduced state for the toxin to function. Oxidation (to disulphide bridges) inactivates the toxin. Examples: tetanolysin, streptolysin O, _ toxin, cereolysin. (18 Nov 1997) |
| thiol beta-lactamase | <enzyme> Active site serine has been mutated to cysteine in e. Coli Registry number: EC 3.5.2.- (26 Jun 1999) |
| thiol-dependent peroxidase | <enzyme> From giardia intestinalis, which lacks glutathione; enzyme can also act with exogenous glutathione Registry number: EC 1.11.1.- Synonym: glutathione-linked thiol peroxidase (26 Jun 1999) |
| thiol endopeptidase | Proteases that have an active thiol group. Includes papain and ficin. (18 Nov 1997) |
| thiol ester | An ester formed from a carboxylic acid and a thiol (i.e., RCO-SR') e.g., acetyl-coenzyme A. (05 Mar 2000) |
| thiol proteinase | Proteases that have an active thiol group. Includes papain and ficin. (18 Nov 1997) |
| acetyl-activating enzyme | 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) |
| acyl-activating enzyme | <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) |
| adaptive enzyme | Inducible enzyme, an enzyme that can be detected in a growing culture of a microorganism, after the addition of a particular substance (inducer) to the culture medium, but was not detectable prior to the addition and can act on the inducer. A prototype is the beta-galactosidase of Escherichia coli, synthesised upon the addition of various galactosides, whether or not these are good substrates. Compare: constitutive enzyme. Synonym: adaptive enzyme. (05 Mar 2000) |
| allosteric enzyme | <biochemistry, chemistry> A regulatory enzyme whose activity is modified by the noncovalent binding of a particular metabolite at a site (the allosteric site) other than the active site. (09 Oct 1997) |
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