| ¿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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| CAAX [box] | protein segment in which C is cysteine, A is usually but not always an aliphatic amino acid, and X i... |
|---|---|
| PA | panic attack; pantothenic acid; paralysis agitans; paranoia; passive aggressive; pathology; patient'... |
| CPI | California Personality Inventory; Cancer Potential Index; congenital palatopharyngeal incompetence; ... |
| CPLM | cysteine-peptone-liver infusion medium |
| CRIP | cysteine-rich intestinal protein |
| CSA | Cysteine sulfinic acid |
|---|---|
| CSAD | Cysteine sulfinic acid decarboxylase |
| ACPI | Acid cysteine proteinase inhibitor |
| TFEC | 1,1,2,2-tetrafluoroethyl-L-cysteine |
| CYS | 1-cysteine |
| cysteine sulfinic acid | -O2S-CH2CH (NH3)+COO-;a natural oxidation product of cysteine; an intermediate in the formation of taurine (via cysteic acid). (05 Mar 2000) |
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| sulfinic acids | Any of the monobasic inorganic or organic acids of sulfur with the general formula rso(oh). (12 Dec 1998) |
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| acetyl CoA-(beta-aminoethyl)-L-cysteine omega-N-acetyltransferase | <enzyme> Forms s-(beta-n-acetyl-aminoethyl)-l-cysteine Registry number: EC 2.3.1.- Synonym: acoac-acetyltransferase, acetyl coenzyme a-(beta-aminoethyl)-l-cysteine omega-n-acetyltransferase (26 Jun 1999) |
| Carica candamarencis glycosylated cysteine proteinase | <enzyme> A glycoprotein from mountain papaya with the carbohydrate moiety bound to asparagine at position 44; has high degree of identity with chymopapain; amino acid sequence has been determined Registry number: EC 3.4.22.- Synonym: cc-iii cysteine proteinase (26 Jun 1999) |
| glutamate-cysteine ligase | <enzyme> One of the enzymes active in the gamma-glutamyl cycle. It catalyses the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. Chemical name: L-Glutamate:L-cysteine gamma-ligase (ADP-forming) Registry number: EC 6.3.2.2 (12 Dec 1998) |
| mercaptolactate-cysteine disulfiduria | Elevated levels of the mixed disulfide of 3-mercaptolactate and cysteine in the urine. (05 Mar 2000) |
| methyl cysteine hydrochloride | Mecysteine hydrochloride;the methyl ester of cysteine hydrochloride; a mucolytic agent. (05 Mar 2000) |
| cysteine | <amino acid> The only amino acid to contain a thiol (SH) group. In intracellular enzymes the unique reactivity of this group is frequently exploited at the catalytic site. In extracellular proteins found only as _ cystine in disulphide bridges or fatty acylated. (18 Nov 1997) |
| cysteine aminopeptidase | <enzyme> Catalyses cysteine-peptide to yield cysteine and peptide Registry number: EC 3.4.11.- (26 Jun 1999) |
| cysteine carboxypeptidase | <enzyme> An enzyme which removes the last peptide bond on a protein (the one at the carboxyl end). Its active site contains the sulphur part of the amino acid cysteine. (09 Oct 1997) |
| cysteine conjugate S-oxidase | <enzyme> Converts s-benzyl-l-cysteine to s-benzyl-l-cysteine sulfoxide; uses o2 and NADPH; may be a flavin-containing monooxygenase Registry number: EC 1.13.12- (26 Jun 1999) |
| cysteine conjugate transaminase | <enzyme> Generates thiopyruvates by deamination of cysteine conjugates leaving the r-s-c bond intact Registry number: EC 2.6.1.- Synonym: cysteine-conjugate alpha-ketoglutarate transaminase (26 Jun 1999) |
| cysteine desulfhydrase | <enzyme> A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyses the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. Chemical name: L-Cystathionine cysteine-lyase (deaminating) Registry number: EC 4.4.1.1 (12 Dec 1998) |
| cysteine desulfurase | <enzyme> Pyridoxal phosphate enzyme which catalyses the formation of l-alanine and elemental sulfur from cysteine; required for full activation of the metalloproteins of azotobacter vinelandii nitrogenase Registry number: EC 4.4.1.- Synonym: nifs gene product, azotobacter, nifs protein, azotobacter (26 Jun 1999) |
| cysteine proteinase | <enzyme> An enzyme that destroys proteins by hydrolysis, turning them back into individual amino acids. (09 Oct 1997) |
| cysteine proteinase inhibitors | Exogenous and endogenous compounds which inhibit cysteine proteinases. (12 Dec 1998) |
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