| ¿µ¹® | alcohol | ÇÑ±Û | ¾ËÄÚ¿Ã |
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| ¼³¸í | ´ë°³ ¿¡Åº¿Ã(ethanol, ethyl alcohol)À» ÁöĪÇÏ´Â ¸»ÀÌ´Ù. ¹°°ú °°ÀÌ ¸¼Àº »öÀÌÁö¸¸ ƯÀÌÇÑ ³¿»õ°¡ ÀÖ°í ²ú´Â Á¡ÀÌ ³·Àº ¾×üÀÌ´Ù. ³óµµ°¡ ³ôÀº °ÍÀº ÀÇ·á¿ë ¶Ç´Â ¼Òµ¶Á¦·Î ¾²ÀÌ°í ³·Àº ³óµµ·Î µÈ °ÍÀº À½·á(¼ú)·Îµµ ÀÌ¿ëµÈ´Ù. |
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| ¿µ¹® | ethyl alcohol | ÇÑ±Û | ¿¡Æ¿¾ËÄÚ¿Ã |
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| ¼³¸í | Áö¹æÁ· Æ÷ȾËÄÚ¿ÃÀÇ Çϳª. °¢Á¾ ¾ËÄÚ¿Ã À½·á ¼Ó¿¡ ÇÔÀ¯µÇ¾î ÀÖ¾î ÁÖÁ¤À̶ó°íµµ Çϰí, ¶Ç ¿¡Åº¿ÃÀ̶ó°íµµ ÇÑ´Ù. º¸Åë ¾ËÄÚ¿ÃÀ̶ó°í Çϸé ÀÌ ¿¡Æ¿¾ËÄÚ¿ÃÀ» °¡¸®Å²´Ù. ¼úÀÇ ¼ººÐÀ¸·Î¼ ¿¹ÀüºÎÅÍ ¾Ë·ÁÁ® ÀÖ¾úÀ¸³ª, ¼úÀÌ ÃëÇÏ´Â ¿øÀÎÀÌ ¿¡Åº¿Ã¿¡ ÀÖ´Ù´Â °ÍÀ» ¾È °ÍÀº 15¼¼±â ÀÌÈÄÀÇ ÀÏÀÌ´Ù. Á¶¼ºÀº óÀ½¿¡ ¶óºÎ¾ÆÁö¿¡³ª N.T. ¼Ò½´¸£ µî¿¡ ÀÇÇØ ÃøÁ¤µÇ°í, °ÔÀÌ·ò»èÀ̳ª J.B. µÚ¸¶ µî¿¡ ÀÇÇØ¼ È®Á¤µÇ¾ú´Ù. ¾ËÄÚ¿ÃÀ̶ó´Â À̸§Àº ¿ø·¡ ´«½ç¿¡ Ä¥ÇÏ´Â Èæ»ö ¾È·áäÔÖù¸¦ °¡¸®Å°´Â ¾Æ¶óºñ¾Æ¾î¿´´Âµ¥. À̰ÍÀÇ ¹Ì¼ÒºÐ¸»À» ¸¸µå´Âµ¥ ½ÂȹýÀ» »ç¿ëÇÑ µ¥¼ ¼úÀ» Áõ·ùÇÏ¿© °¡¿¬¼º ¿¢½º¸¦ ¸¸µå´Â °ÍÀ¸·Î ÀüÈï®ûùÇϰí, À̰ÍÀÌ ´Ù½Ã Áõ·ù¹°À» °¡¸®Å°´Â ¸»ÀÌ µÇ¾ú´Ù. ¾ËÄÚ¿ÃÀ̶ó´Â ¸»ÀÌ ¿¡Åº¿ÃÀ» °¡¸®Å°°Ô µÇ°í, ´Ù½Ã ¾ËÄÚ¿Ã Àü¹ÝÀ» °¡¸®Å°°Ô µÈ °ÍÀº 19¼¼±â ÀÌÈÄÀÇ ÀÏÀÌ´Ù. ¿¡Åº¿ÃÀ» º¹¿ëÇÏ¸é ´ë³úÀÇ Á¦¾î±â´ÉÀÌ ¾ïÁ¦µÇ¾î ÈïºÐ»óŰ¡ µÇ°í, ÀÌ¾î¼ ÁßÃ߽ŰæÀÌ ¾ïÁ¦µÈ´Ù. ¹«»öÅõ¸íÇÑ Èֹ߼º ¾×ü. ƯÀ¯ÇÑ ³¿»õ¿Í ¸ÀÀ» °¡Áö¸ç, ÀÎü¿¡ Èí¼öµÇ¸é ÈïºÐÀ̳ª ¸¶Ãë ÀÛ¿ëÀ» ÀÏÀ¸Å²´Ù. ÈÇоàǰÀÇ ÇÕ¼º ¿ø·á, ¿ëÁ¦, ¿¬·á, ¾ËÄڿüº À½·á µûÀ§·Î ¾´´Ù. ¾ËÄÚ¿ÃÀº °£¼¼Æ÷¿¡ Á¸ÀçÇÏ´Â ¾ËÄÚ¿ÃÅ»¼ö¼ÒÈ¿¼Ò(alcohol dehydrogenase)°¡ ´ë»çÇÑ´Ù. ±Þ¼º Áßµ¶ Áõ»óÀº Ç÷Áß ¾ËÄÚ¿Ã ³óµµ¿Í ºñ·ÊÇÑ´Ù. Ç÷Áß ¾ËÄÚ¿Ã ³óµµ°¡ ³ô¾ÆÁú¼ö·Ï ÁßÃ߽Űæ°è´Â ¾ïÁ¦µÇ¾î Ç÷Áß ³óµµ°¡ 3.5~4.5mg/mLÀ̸é È¥¼ö¿¡ ºüÁ® »ç¸ÁÇÒ ¼öµµ ÀÖ´Ù. |
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| ¿µ¹® | fetal alcohol syndrome | ÇÑ±Û | žƾËÄÚ¿ÃÁõÈıº |
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| ¼³¸í | ÀӽűⰣ Áß ¸¸¼ºÀûÀ¸·Î ¾ËÄÚ¿ÃÀ» ¼·ÃëÇÑ ¿©ÀÚ¿¡°Ô¼ ÅÂ¾î³ ¿µ¾Æ¿¡°Ô ³ªÅ¸³ª´Â ÇüŹ߻ýÀÇ ÀÌ»óÀ» ³ªÅ¸³»´Â ÁõÈıºÀ¸·Î¼ À§ÅλÀ¹ßÀ°ºÎÀü, ¾Õ¸Ó¸®¿Í ¾Æ·¡ÅÎÀÇ µ¹Ãâ, ªÀº°Ë¿, ÀÛÀº¾È±¸Áõ, ´«±¸¼®ÁÖ¸§, ½ÉÇÑ ¼ºÀåÁö¿¬, Á¤½ÅÁöü µîÀ» ³ªÅ¸³½´Ù. |
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| GDH | glucose dehydrogenase; glutamate dehydrogenase; glycerophosphate dehydrogenase; glycol dehydrogenase... |
|---|---|
| LADH | lactic acid dehydrogenase; liver alcohol dehydrogenase |
| D-A | donor-acceptor |
| EDA | electrodermal activity; electrodermal audiometry; electrolyte-deficient agar; electron donor accepto... |
| MAP | malignant atrophic papulosis; mandibular angle plane; maturation-activated protein; maximal aerobic ... |
| A | D)-acceptor |
|---|---|
| ADH | 3-alcohol dehydrogenase |
| ADH3 | Alcohol dehydrogenase 3 |
| ADH1 | Alcohol dehydrogenase-1 |
| ADH2 | Alcohol dehydrogenase-2 |
| alcohol dehydrogenase (acceptor) | An oxidoreductase that reversibly converts primary alcohols to aldehydes with an H acceptor other than NADP+. (05 Mar 2000) |
|---|
| alcohol dehydrogenase | <enzyme> An enzyme that catalyses reversibly the final step of alcoholic fermentation by reducing an aldehyde to an alcohol. In the case of ethanol, acetaldehyde is reduced to ethanol in the presence of NADH and hydrogen. The enzyme is a zinc protein which acts on primary and secondary alcohols or hemiacetals. Chemical name: Alcohol:NAD+ oxidoreductase Registry number: EC 1.1.1.1 (12 Dec 1998) |
|---|---|
| alcohol dehydrogenase (NADP+) | An oxidoreductase reversibly converting alcohols to aldehydes (or ketones) with NAD(P)+ as H acceptor. Synonym: aldehyde reductase, DPNH aldehyde transhydrogenase. (05 Mar 2000) |
| benzyl alcohol dehydrogenase | <enzyme> Catalyses the oxidation of benzyl alcohol to yield benzaldehyde Registry number: EC 1.1.1.- (26 Jun 1999) |
| cinnamyl alcohol dehydrogenase | <enzyme> Nadp-dependent Registry number: EC 1.1.1.195 Synonym: cad2 protein (26 Jun 1999) |
| coenzyme F420-dependent alcohol dehydrogenase | <enzyme> From methanogenium liminatans; catalyses oxidation of various secondary and cyclic alcohols to the corresponding ketones and the reverse reaction Registry number: EC 1.1.99.- Synonym: f(420) alcohol dehydrogenase (26 Jun 1999) |
| coniferyl alcohol dehydrogenase | <enzyme> Leads to the formation of the monomers of lignins, requires nadp+ Registry number: EC 1.1.1.- (26 Jun 1999) |
| 4-sulfobenzyl alcohol dehydrogenase | <enzyme> Catalyses the formation of 4-sulfobenzaldehyde from 4-sulfobenzyl alcohol; amino acid sequence given in first source Registry number: EC 1.1.1.- Synonym: p-sulfobenzyl alcohol dehydrogenase, tsac protein, tsac gene product (26 Jun 1999) |
| long-chain-alcohol dehydrogenase | <enzyme> Catalyses reversibly the oxidation of a long-chain alcohol in the presence of nad to a long-chain acid anion and NADH Registry number: EC 1.1.1.192 Synonym: fatty alcohol-nad+ oxidoreductase (26 Jun 1999) |
| acceptor | A compound that will take up a chemical group (e.g., an amine group, a methyl group, a carbamoyl group) from another compound (the donor); under the action of alanine transaminase, l-glutamic acid is an amine donor while pyruvic acid is an amine acceptor. Origin: L. Ac-cipio, pp. -ceptus, to accept (05 Mar 2000) |
| acceptor control | <biochemistry> The regulation of the respiration rate, governed by ADP's ability to be a phosphate group acceptor. (06 May 1997) |
| acceptor RNA | rNA |
| acceptor site | The ribosomal binding site for the aminoacyl-tRNA during protein synthesis. (05 Mar 2000) |
| acceptor splicing site | Boundary between the right end of an intron and the left end of the adjacent exon. Synonym: acceptor splicing site. (05 Mar 2000) |
| phenylglyoxylate - acceptor oxidoreductase | <enzyme> Requires coenzyme a; converts phenylglyoxylate to benzoyl-CoA with release of co2 Registry number: EC 1.2.99.- Synonym: phenylglyoxylate oxidoreductase (acylating) (26 Jun 1999) |
| proton acceptor | <chemistry> A base, an anionic substance that acceptsa proton during an acid-basereaction. (09 Oct 1997) |
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