| ¿µ¹® | deoxyribonucleic acid (DNA) | ÇÑ±Û | µ¥¿Á½Ã¸®º¸ÇÙ»ê |
|---|---|---|---|
| ¼³¸í | ÇÙ»êÀÇ ÀÏÁ¾À¸·Î DNA¶ó°íµµ ÇÑ´Ù. DeoxyribonucleotideÀÇ ÁßÇÕüÀ̸ç À¯ÀüÀÚÀÇ ÈÇÐÀû º»Ã¼ÀÌ´Ù. RNA¹ÙÀÌ·¯½º ÀÌ¿ÜÀÇ ¸ðµç »ý¹°Àº DNA¸¦ À¯ÀüÀÚ·Î Áö´Ï°í ÀÖ´Ù. µð¿Á½Ã¸®º¸´ºÅ¬·¹¿ÀƼµå(deoxyribonucleotide)´Â ¿°±â¿Í ´ç(2'-deoxy-D-ribose)°ú ÀλêÀ¸·Î ÀÌ·ç¾îÁø´Ù. ¿°±â´Â ¾Æµ¥´Ñ(adenine), ±¸¾Æ´Ñ(guanine), Ƽ¹Î(thymine)¹× ½ÃÅä½Å(cytosine)ÀÇ 4°¡ÁöÀ̸ç, À̰ÍÀº ´ç¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÎ»ê ¿ª½Ã ´çÀÇ ÇÑ ºÎºÐ¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÌ deoxyribonucleotideÀÇ ´çÀº ´Ù¸¥ deoxy- ribonucleotideÀÇ ´ç°ú ÀλêÀ» »çÀÌ¿¡ ³õ°í °áÇÕÀ» ÇÏ°Ô µÇ¾î ÇϳªÀÇ ±ä »ç½½À» Çü¼ºÇÏ°Ô µÈ´Ù. Áï ´ç°ú ÀλêÀÌ ÁÖÃàÀÌ µÇ¾î¼ deoxyribonucleotideÀÇ ±ä »ç½½À» ¸¸µç´Ù. ÀÌ deoxyribonucleotideÀÇ »ç½½ µÎ °³´Â °¢°¢ deoxyribonucleotide¿¡ ºÎÂøµÇ¾î ÀÖ´Â ¿°±âµéÀÌ °áÇÕÀ» ÇÏ¿© µÎ °³ÀÇ »ç½½ÀÌ °áÇյǾî ÀÖ´Â ÀÌÁß³ª¼± ±¸Á¶¸¦ ¸¸µé°Ô µÈ´Ù. 4°¡Áö ¿°±â ¾Æµ¥´ÑÀº Ƽ¹Î°ú °áÇÕÀ» Çϰí, ½ÃÅä½Å°ú °áÇÕÀ» ÇÏ°Ô µÈ´Ù. Áï ´ç°ú ÀλêÀº ±ä »ç½½À» ¸¸µå´Â ¿ªÇÒÀ» ÇÏ°í ±ä »ç½½¿¡ ºÎÂøµÈ ¿°±âµéÀÇ °áÇÕ¿¡ ÀÇÇØ¼ µÎ °³ÀÇ ±ä »ç½½Àº ¼·Î ºÙ¾î¼ ÀÌÁß³ª¼± ±¸Á¶¸¦ ¸¸µç´Ù. DNAÀÇ À¯ÀüÁ¤º¸´Â ¿°±â¿¡ ÀúÀåµÈ´Ù. 4°³ÀÇ ¿°±âÀÇ Á¶ÇÕ°ú ¹è¿ÀÌ À¯ÀüÁ¤º¸¸¦ º¸°üÇÏ´Â ÇϳªÀÇ ¾ÏÈ£ ¿ªÇÒÀ» ÇàÇÏ°Ô µÈ´Ù. |
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| ¿µ¹® | retinoic acid | ÇÑ±Û | ·¹Æ¼³ë»ê |
|---|---|---|---|
| ¼³¸í | C20H28O2. ºñŸ¹Î AÀÇ ¾ËÄڿñ⸦ ¾Ëµ¥È÷µå·Î »êÈÇÑ ÈÄ ´Ù½Ã Ä«¸£º¹½Ç»êÀ¸·Î »êÈÇÏ¿© ¾òÀº »ê. ¹ß»ýÁßÀÇ ¼¼Æ÷¿¡ ÀÛ¿ëÇÏ¿© ÇüŸ¦ ¸¸µå´Âµ¥ °ü¿©ÇÑ´Ù. |
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| ¿µ¹® | ribonucleic acid | ÇÑ±Û | ¸®º¸ÇÙ»ê |
|---|---|---|---|
| ¼³¸í | Ribonucleotide monomer·Î ÀÌ·ç¾îÁø ÇÙ»êÀ¸·Î ¿°±â, ´ç, ÀλêÀ¸·Î ±¸¼ºµÈ´Ù. ¿°±â´Â adenine, guanine, cytosine, uracilÀÇ 4Á¾·ù°¡ ÀÖÀ¸¸ç, ´çÀº 5ź´çÀÌ´Ù. RNA´Â DNA¸¦ ÁÖÇüÀ¸·Î ÇÏ¿© »óº¸ÀûÀ¸·Î °áÇÕ, Çü¼ºµÇ¸ç ´Ü¹éÁúÀ» ¸¸µé¾î³»´Â µ¥¿¡ ÀÖ¾î Áß¿äÇÑ ¿ªÇÒÀ» ÇÑ´Ù. Àü·É RNA(mRNA)´Â ´Ü¹éÁú ÇÕ¼º¿¡ ÀÖ¾î °¡Àå ±âº»ÀÌ µÇ´Â DNAÀÇ ¼¿À» »óº¸ÀûÀ¸·Î ¿Å°Ü ¹Þ¾Æ Àü´ÞÇÏ´Â Àü·É±¸½ÇÀ» ÇÏ´Â RNA. ¸®º¸¼Ø RNA(rRNA) ¸®º¸¼ØÀ» Çü¼ºÇÏ´Â 4°¡Áö RNA»ç½½(28S, 18S, 5.8S, 5S·Î ±¸¼º). Àü´Þ RNA(tRNA) ƯÁ¤ ¾Æ¹Ì³ë»êÀ» ÇÑÂÊ ³¡¿¡ Áö´Ï°í »óº¸Àû ¼¿ÀÇ mRNA¿Í ÀϽÃÀû °áÇÕÀ» ÀÌ·ç¸ç ´Ü¹éÁú ÇÕ¼º¿¡ Á÷Á¢ ±â¿©ÇÏ´Â RNAÀÌ´Ù. |
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| ¿µ¹® | acid | ÇÑ±Û | »ê |
|---|---|---|---|
| ¼³¸í | ¹°¿¡ ³ì¾ÒÀ» ¶§ ÀÌ¿ÂÈÇÏ¿© ¼ö¼Ò ÀÌ¿ÂÀ» ¸¸µå´Â ¹°Áú. ½Å¸ÀÀÌ ³ª°í û»ö ¸®Æ®¸Ó½º Á¾À̸¦ ºÓ°Ô º¯È½ÃŰ¸ç ¿°±â¿ÍÀÇ ÁßÈ ¹ÝÀÀ¿¡ ÀÇÇÏ¿© ¹°°ú ¿°À» ¸¸µé°í ÀÌ¿ÂÈ ¿¿¡¼ ¼ö¼Òº¸´Ù ¾Õ¿¡ ÀÖ´Â ±Ý¼Ó°ú ¹ÝÀÀÇÏ¿© ¿°À» ¸¸µé¸é¼ ¼ö¼Ò¸¦ ¹ß»ý½ÃŲ´Ù. ¼ö¼Ò ¿øÀÚ¸¦ ÀÌ¿ÂÈÇÏ´Â ÈûÀÇ °¾à¿¡ µû¶ó °»ê°ú ¾à»êÀ¸·Î ³ª´¶´Ù. |
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| ¿µ¹® | acetic acid | ÇÑ±Û | ¾Æ¼¼Æ®»ê, ÃÊ»ê |
|---|---|---|---|
| ¼³¸í | ºÐÀÚ½ÄÀº C2H4O2, ºÐÀÚ·® 60.05ÀÇ Àú±Þ Áö¹æ»êÀÌ´Ù. CH3COOHÀÇ ±¸Á¶½ÄÀ» °¡Áø ¹«»ö¾×ü·Î 16.7¡É¿¡¼ ³ì°í 118.0¡É¿¡¼ ²ú´Â´Ù. ½ÄÃÊÀÇ ½Å¸ÀÀ» ³»´Â °ÍÀ̰í, ³óÃàµÈ °ÍÀ» ºùÃÊ»êÀ̶ó ÇÑ´Ù. »ó¿Â¿¡¼´Â ¾×üÀÌ¸ç ¼ö¿ë¾×Àº ¾à»ê¼ºÀÌ´Ù. »ýü³»¿¡¼´Â ÀϹÝÀûÀ¸·Î ¾Æ¼¼Æ¿ CoA·Î Á¸ÀçÇÏ¸ç ¾Æ¼¼Æ¿±âÀÇ °ø±Þ¿øÀÌ µÇ´Â ¿Ü¿¡ Áö¹æ»êÀ̳ª ½ºÅ×·ÎÀÌµå µîÀÇ »ý¼ºÀç·á·Î Áß¿äÇÏ´Ù. ¾Æ¼¼Æ¿ CoA·ÎºÎÅÍ´Â ÄÉÅæÃ¼°¡ ÇÕ¼ºµÇ¸ç Á¶Á÷ÀÇ ¿¡³ÊÁö¿øÀÌ µÈ´Ù. |
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| PA | panic attack; pantothenic acid; paralysis agitans; paranoia; passive aggressive; pathology; patient'... |
|---|---|
| HMOX | heme oxygenase |
| HTOR | 5-hydroxytryptamine oxygenase regulator |
| MHO | microsomal heme oxygenase |
| MO | macroorchidism; manually operated; Master of Obstetrics; Master of Osteopathy; medical officer; mesi... |
| COX | Cyclo-oxygenase |
|---|---|
| COX 2 | cyclo-oxygenase |
| COX-1 | Cyclo-oxygenase-1 |
| COX-2 | Cyclo-oxygenase-type-2 |
| RuBisCO | D-ribulose-1,5-bisphosphate carboxylase/oxygenase |
| 2,4,5-trichlorophenoxyacetic acid oxygenase | <enzyme> Converts the herbicide 2,4,5-t to 2,4,5-trichlorophenol; genbank u11420 Registry number: EC 1.13.99.- Synonym: 2,4,5-t oxygenase (26 Jun 1999) |
|---|
| 5-pyridoxic acid oxygenase | <enzyme> From arthrobacter cr-7 grown on pyridoxine; forms alpha-hydroxymethyl-alpha'-(n-acetylaminomethylene)succinic acid; uses NADPH + fad; involved in vitamin b6 degradation Registry number: EC 1.4.12.- (26 Jun 1999) |
|---|---|
| alpha-ketoisocaproate oxygenase | <enzyme> From rat liver cytosol; oxidatively decarboxylates and hydroxylates alpha-ketoisocaporate to form beta-hydroxyisovalerate; requires fe(2+) and thiol; activated by ascorbate Registry number: EC 1.13.11.- Synonym: 2-ketoisocaproate oxygenase, alpha-ketoisocaproate dioxygenase (26 Jun 1999) |
| anhydrotetracycline oxygenase | <enzyme> Streptomyces aureofaciens enzyme catalyzing penultimate reaction of tetracycline biosynthesis, hydration of anhydrotetracycline to dehydrotetracycline Registry number: EC 1.14.99.- (26 Jun 1999) |
| aniline oxygenase | <enzyme> Converts substituted anilines to the corresponding catechols Registry number: EC 1.14.99.- (26 Jun 1999) |
| benzene mono-oxygenase | <enzyme> Cytochrome p-450-dependent; forms benzene oxide Registry number: EC 1.13.12.- (26 Jun 1999) |
| bromomethane mono-oxygenase | <enzyme> Enzyme responsible for methane oxidation in vivo Registry number: EC 1.13.12.- (26 Jun 1999) |
| ribulose-1,5-bisphosphate carboxylase-oxygenase large subunit epsilonN-methyltransferase | <enzyme> An aspect of EC 2.1.1.43; trimethylates lys-14 of rubisco Registry number: EC 2.1.1.- Synonym: rubisco lsmt, rubisco large subunit lysine n-methyltransferase (26 Jun 1999) |
| ribulosebisphosphate carboxylase-oxygenase activase | <chemical> Requires ATP; amino acid sequence given in first source Synonym: rubisco activase, rca protein (26 Jun 1999) |
| phthalate oxygenase reductase | <enzyme> Flavoenzyme which transfers electrons from NADH to the iron-sulfur centre of phthalate oxygenase Registry number: EC 1.- Synonym: phthalate dioxygenase reductase (26 Jun 1999) |
| porphobilinogen oxygenase | <enzyme> Porphobilinogen is converted to 5-oxo-porphobilinogen Registry number: EC 1.13.- (26 Jun 1999) |
| haem oxygenase (decyclizing) | <enzyme> A mixed function oxidase enzyme which during haemoglobin catabolism catalyses the degradation of haem to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. Chemical name: Haem,hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating) Registry number: EC 1.14.99.3 (12 Dec 1998) |
| cyclohexanone oxygenase | <enzyme> Requires NADPH and oxygen, forms epsilon-caprolactone Registry number: EC 1.14.13.- Synonym: cyclohexanone monooxygenase, flavoenzyme cyclohexanone monooxygenase (26 Jun 1999) |
| sulfur oxygenase reductase | <enzyme> From desulfurolobus ambivalens; in the presence of oxygen but not under a hydrogen atmosphere simultaneously produces sulfite, thiosulfate, and hydrogen sulfide from sulfur; inhibited by sulfhydryl reagents, fad, ferrous and ferric ions Registry number: EC 1.8.- Synonym: sor gene product (sulfur oxygenase reductase) (26 Jun 1999) |
| dihydroxynaphthalene oxygenase | <enzyme> Also catalyses ring cleavage in an extradiol mode: between a hydroxylated and an adjacent non-hydroxylated carbon Registry number: EC 1.13.- Synonym: 1,2-dihydroxynaphthalene dioxygenase (26 Jun 1999) |
| questin oxygenase | <enzyme> Catalyses the conversion of questin to desmethylsulochrin; isolated from aspergillus terreus Registry number: EC 1.14.13.- (26 Jun 1999) |
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