| ¿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'... |
|---|---|
| AA | abdominal aorta; acetic acid; achievement age; active alcoholic; active assistive [range of motion];... |
| OA | obstructive apnea; occipital artery; occipito-anterior; occiput anterior; octanoic acid; ocular albi... |
| PAA | partial agonist activity; phenylacetic acid; phosphonoacetic acid; physical abilities analysis; plas... |
| NP | Nucleoside Phosphorylase |
| GP | Glycogen Phosphorylase |
|---|---|
| MTAP | Methylthioadenosine phosphorylase |
| NP | Nucleoside phosphorylase |
| PHK | Phosphorylase kinase |
| PD-ECGF/TP | Platelet-derived endothelial cell growth factor/thymidine phosphorylase |
| orotidylic acid phosphorylase | <enzyme> The enzyme catalyzing the formation of orotidine-5'-phosphoric acid (orotidylic acid) from orotic acid and 5-phosphoribosyl-1-pyrophosphate in the course of pyrimidine nucleotide biosynthesis. Chemical name: Orotidine-5'-phosphate:pyrophosphate phospho-alpha-D-ribosyltransferase Registry number: EC 2.4.2.10 (12 Dec 1998) |
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| orotidylic acid | Orotidine 5'-monophosphate;an intermediate in the biosynthesis of the pyrimidine nucleosides (cytidine and uridine) that are found in nucleic acids. Synonym: orotidine 5'-monophosphate. (05 Mar 2000) |
|---|---|
| orotidylic acid decarboxylase | <enzyme> An enzyme that catalyses the conversion of OMP to UMP and CO2; a defect or inhibition of this enzyme will result in orotic aciduria and orotidinuria; this enzyme is a part of pyrimidine biosynthesis. Compare: uridylic acid synthase. Synonym: OMP decarboxylase. (05 Mar 2000) |
| orotidylic acid pyrophosphorylase | <enzyme> The enzyme catalyzing the formation of orotidine-5'-phosphoric acid (orotidylic acid) from orotic acid and 5-phosphoribosyl-1-pyrophosphate in the course of pyrimidine nucleotide biosynthesis. Chemical name: Orotidine-5'-phosphate:pyrophosphate phospho-alpha-D-ribosyltransferase Registry number: EC 2.4.2.10 (12 Dec 1998) |
| alpha,alpha-trehalose phosphorylase | <enzyme> Chemical name: alpha-d-glucopyranosyl-alpha-d-glucopyranose orthophosphate glucosyltransferase Registry number: EC 2.4.1.64 Synonym: trehalose phosphorylase (26 Jun 1999) |
| alpha-glucan phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| maltodextrin phosphorylase | <enzyme> From E coli Registry number: EC 2.4.1.- Synonym: e350a (26 Jun 1999) |
| GDPmannose phosphorylase | <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate. Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases Registry number: EC 2.7.7.13 Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein (26 Jun 1999) |
| cellodextrin phosphorylase | <enzyme> Reverse reaction is used to synthesise cellodextrins Registry number: EC 2.4.1.49 (26 Jun 1999) |
| glycogen phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| phosphorylase | <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase). (21 Jun 2000) |
| phosphorylase a | <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase b | <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP. Registry number: EC 2.4.1.- (12 Dec 1998) |
| phosphorylase kinase | <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle. (18 Nov 1997) |
| phosphorylase kinase phosphatase | <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16 Registry number: EC 3.1.3.- (26 Jun 1999) |
| phosphorylase phosphatase | <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. Chemical name: (Phosphorylase a) phosphohydrolase Registry number: EC 3.1.3.17 (12 Dec 1998) |
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