| ¿µ¹® | allergic disease | ÇÑ±Û | ¾Ë·¹¸£±âº´ |
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| ¼³¸í | ³ÐÀº ¶æÀ¸·Î´Â IÇü, IIÇü, IIIÇü ¹× IVÇüÀÇ ¾Ë·¹¸£±â ¹ÝÀÀ¿¡ ÀÇÇØ¼ »ý±â´Â ¸ðµç º´À» °¡¸®Å²´Ù. ±×·¯³ª º¸Åë ¾Ë·¹¸£±âº´À̶ó°í Çϸé Á¼Àº ¶æÀ» °¡¸®Å°´Â °æ¿ì°¡ ¸¹°í, IÇüÀÇ ¾Ë·¹¸£±â¹ÝÀÀ¿¡ ÀÇÇØ¼ »ý±â´Â °ÍÀ» °¡¸®Å²´Ù. Áï ¾ÆÅäÇǺ´°ú ¸¶Âù°¡Áö ¶æÀ¸·Î ÇØ¼®µÇ´Â °æ¿ì°¡ ¸¹°í, ±â°üÁöõ½Ä, ¾Ë·¹¸£±âÄÚ¿°, ¾Ë·¹¸£±âÁ¡¸·¿°, µÎµå·¯±â, ¾Æ³ªÇʶô½Ã½º µîÀÌ ¿©±â¿¡ ¼ÓÇÑ´Ù. |
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| ¿µ¹® | Alzheimer's disease | ÇÑ±Û | ¾ËÃ÷ÇÏÀ̸Ӻ´ |
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| ¼³¸í | ÅðÇ༺ ³úº´. ³ëÀο¡¼ÀÇ Ä¡¸ÅÀÇ ¿øÀÎ Áß °¡Àå ÈçÇÑ ÇüÅÂÀÌ´Ù. º´¸®Á¶Á÷ÇÐÀûÀ¸·Î´Â ³úÀÇ Àü¹ÝÀûÀÎ À§Ãà, ³ú½ÇÀÇ È®Àå, ½Å°æ¼¶À¯ÀÇ ´Ù¹ß¼º º´ÅÍ(½Å°æ¼¶À¯µÚƲ¸²)¿Í ³ëÀιÝ(neuritic plaque) µîÀÌ Æ¯Â¡ÀÌ´Ù. ÀÓ»óÀûÀΠƯ¡Àº Á¡ÁøÀûÀÎ ±â¾ï-ÆÇ´Ü-¾ð¾î´É·Â µî ÁöÀûÀÎ ±â´ÉÀÇ °¨Åð¿Í ÀÏ»ó»ýȰ´É·Â-ÀΰÝ-Çൿ¾ç»óÀÇ Àå¾ÖÀÌ´Ù. º´¿¡ °É¸®¸é Ãʱ⿡´Â À̸§-³¯Â¥-Àå¼Ò¿Í °°Àº °ÍµéÀÌ ±â¾ï¿¡¼ »ç¶óÁö°í, ½ÉÇØÁö¸é ÈÀå½ÇÀ» °¡°Å³ª ¿ä¸®¸¦ Çϰųª ½ÅÀ» ½Å´Â ÀÏ µîÀÇ ÀÏ»ó»ýȰÁ¶Â÷µµ ÀØ°Ô µÈ´Ù. µ¿½Ã¿¡ ¿ì¿ïÁõ¼¼³ª ÀΰÝÀÇ È²Æó, °ÝÇÑ Çൿ µîÀÇ Á¤½ÅÀÇÇÐÀûÀÎ Áõ¼¼µµ µ¿¹ÝµÈ´Ù. ÀÌ·¯ÇÑ Áõ¼¼µéÀÌ Á¡ÀüÀûÀ¸·Î ÁøÇàµÇ¾î °á±¹Àº Á×À½¿¡ À̸£°Ô µÈ´Ù. ¹ßº´ ÈÄ ¼¼È÷ Á×À½¿¡ À̸£´Â ±â°£Àº 6~8³â Á¤µµÀÌÁö¸¸ »ç¶÷¿¡ µû¶ó 20³âÀÌ ³Ñ´Â °æ¿ìµµ ÀÖ´Ù. |
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| ¿µ¹® | Addison disease | ÇÑ±Û | ¾Öµð½¼º´ |
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| ¼³¸í | ºÎ½Å°ÑÁúÀÇ º´ÅÍ·Î ÀÎÇÏ¿© ºÎ½Å°ÑÁúÀÇ È£¸£¸óÀÌ ³ª¿ÀÁö ¸øÇؼ »ý±â´Â º´. ¿ì¸®³ª¶ó¿¡¼ °¡Àå ¸¹Àº ¿øÀÎÀº °áÇÙÀÌ´Ù. ¾Öµð½¼º´¿¡¼´Â ºÎ½Å°ÑÁúÀÇ ÆÄ±«¿¡ ÀÇÇØ¼ ºÎ½Å°ÑÁú¿¡¼ ³ª¿À´Â È£¸£¸óÀÌ ¾ø¾îÁö¹Ç·Î ÄáÆÏ¿¡¼ ¹°ÀÇ Èí¼öÀå¾Ö·Î ÀÎÇØ Å»¼ö»óŰ¡ Áö¼ÓµÇ¸ç, ½ºÆ®·¹½º È£¸£¸óÀÇ °áÇÌ¿¡ ÀÇÇØ¼ ¸¸¼ºÇÇ·Î, üÁß°¨¼Ò µîÀÇ Áõ»óÀÌ »ý±â¸ç, ³úÇϼöü¿¡¼ ºÎ½Å°ÑÁúÀÇ ºÐºñ¸¦ ³ôÀÌ´Â ºÎ½Å°ÑÁúÀÚ±ØÈ£¸£¸óÀÇ °ú´Ù ºÐºñ·Î ÀÎÇØ¼ °°ÀÌ ºÐºñµÇ´Â ¸á¶ó´ÑÀÚ±ØÈ£¸£¸ó¿¡ ÀÇÇØ ¾ó±¼°ú ÀÔ¼ú¿¡ °úµµÇÑ »ö¼ÒÀÇ Ä§ÂøÀ» º¼ ¼ö ÀÖ´Ù. |
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| ¿µ¹® | inflammatory bowel disease | ÇÑ±Û | ¿°Áõ¼ºÃ¢ÀÚº´ |
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| ¼³¸í | À§Àå°üÀ» ħ¹üÇÏ´Â Á¤È®ÇÑ ¿øÀÎÀÌ ¹àÇôÁöÁö ¾ÊÀº ¸¸¼ºÀûÀÎ ¿°Áõ¼º ÁúȯÀ» ¸»ÇÑ´Ù. Å©°Ô ¡®±Ë¾ç¼º ´ëÀå¿°¡¯(ulcerative colitis)°ú ¡®Å©·Ðº´¡¯(Crohn's disease)ÀÇ µÎ Á¾·ù·Î ±¸ºÐµÈ´Ù. ¹éÀÎ, À¯ÅÂÀο¡ ¸¹°í ÈæÀÎÀ̳ª µ¿¾çÀο¡´Â µå¹°Áö¸¸ µ¿¾çÀο¡¼ Á¡Â÷ Áõ°¡Ãß¼¼¿¡ ÀÖ´Ù. È£¹ß¿¬·ÉÀº 15~35¼¼ »çÀÌÀÌ´Ù. Áõ»óÀº ¡®±Ë¾ç¼º ´ëÀå¿°¡¯ÀÇ °æ¿ì, ¼³»ç(Ç÷º¯ ¹× Á¡¾×º¯), µÚ¹«Á÷, º¹Åë, º¹ºÎ¾ÐÅë, üÁß°¨¼Ò µîÀÌ ÁÖ·Î ³ªÅ¸³ª¸ç ¡®Å©·Ðº´¡¯¿¡¼´Â ¼³»ç¿Í üÁß°¨¼Ò, ¿ìÇϺ¹ºÎ Á¾·ù, Ç×¹®ÁÖÀ§ ÀÌ»ó, º¹ºÎ¾ÐÅë µîÀÌ ³ªÅ¸³´Ù. Áø´ÜÀº º´·Â°ú ¹æ»ç¼±ÇÐÀû °Ë»ç, Á÷Àå°æ ¹× ´ëÀå ³»½Ã°æ°Ë»ç, Á÷Àå ¹× ´ëÀåÀÇ Á¶Á÷°Ë»ç·Î Çϸç Ä¡·á´Â ³»°úÀûÀÎ Ä¡·á°¡ ¿øÄ¢À̳ª ³»°úÀû Ä¡·á¿¡ µèÁö ¾Ê°Å³ª ÇÕº´ÁõÀÌ »ý±æ °æ¿ì¿¡´Â ¿Ü°úÀû Ä¡·á¸¦ ½ÃÇàÇÑ´Ù. ¡®±Ë¾ç¼º ´ëÀå¿°¡¯ÀÇ °æ¿ì¿¡´Â ¡®´ëÀå¾Ï¡¯À» ¿¹¹æÇϱâ À§Çؼ ¿Ü°úÀû Ä¡·á¸¦ Çϱ⵵ ÇÑ´Ù. ¡®±Ë¾ç¼º ´ëÀå¿°¡¯°ú ¡®Å©·Ð º´¡¯¿Ü¿¡ ¿°Áõ¼º âÀÚº´¿¡ ¼ÓÇÏ´Â ¡®º£Ã¼Æ® º´¡¯Àº Àç¹ß¼º ±¸°³» ±Ë¾ç, ÇǺΠº´º¯, ¾È±¸ºÎ ¿°Áõ, ¿ÜÀ½ºÎ ±Ë¾ç, °üÀý¿° Áõ»ó, À§Ã¢ÀÚ°ü Áõ»ó(º¹Åë, ÀåÃâÇ÷), ºÎ°íȯ¿° µîÀÇ Áõ»óÀ» ³ªÅ¸³»´Âµ¥ Áø´Ü°ú Ä¡·á´Â ¡®±Ë¾ç¼º ´ëÀå¿°¡¯, ¡®Å©·Ð º´¡¯°ú ºñ½ÁÇÏ´Ù. |
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| ¿µ¹® | Wilson's disease | ÇÑ±Û | Àª½¼º´ |
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| ¼³¸í | °£À̳ª ³ú¿¡ ±¸¸®°¡ ºñÁ¤»óÀûÀ¸·Î ½×¿© ÀϾ´Â À¯Àü¼º ´ë»çº´. °£°æÈÁõÀ̳ª ½Å°æ Áõ»óÀÌ µû¸£´Âµ¥, ¼Õ ¶³¸²À̳ª ¾ð¾î Àå¾Ö°¡ »ý±â°í ´«ÀÇ °¢¸· ÁÖÀ§¿¡ ³ì°¥»ö °í¸®°¡ ³ªÅ¸³´Ù. ¿µ±¹ÀÇ ½Å°æ°ú ÀÇ»ç Àª½¼(Wilson)ÀÌ ºÐ·ùÇÑ º´ÀÌ´Ù. º¸Åë¿°»öü ¿¼ºÀ¸·Î À¯ÀüµÈ´Ù. Çѱ¹¿¡¼µµ ÇöÀç±îÁö 50¿© ¿¹°¡ º¸°íµÇ¾î ÀÖ´Ù. À̺´Àº º¸Åë¿°»öü ¿¼ºÀ¸·Î À¯ÀüµÇ¸ç, ATP7B¶ó´Â Àª½¼º´ À¯ÀüÀÚ°¡ 13¹ø ¿°»öü¿¡ À§Ä¡ÇÑ´Ù. Ư¡À¸·Î ±¸¸®°¡ °£, ³ú ¹× °¢¸·¿¡ ÃàÀûÇÏ¿© ¸¸¼º °£¿° ¶Ç´Â °£°æÈ¿Í °°Àº °£¼Õ»óÀ» ÀÏÀ¸Å°°í, ³ú ƯÈ÷ ·»ÁîÇÙÀÇ ÅðÇà º¯È¿Í °¢¸·¸ð¼¸®¿¡ ³ì°¥»öÀÇ Kayser-Fleischer °í¸®¸¦ Çü¼ºÇÑ´Ù. ÀÓ»óÁõ»óÀÇ ¹ßÇöÀº º¸Åë 5~15¼¼¿¡ ½ÃÀÛÇϴµ¥ 30~40¼¼°¡ µÇµµ·Ï Áõ»óÀÌ ¾øÀ» ¼öµµ ÀÖ´Ù. |
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| chain reflex | A series of reflexs, each serving as a stimulus for the next. (05 Mar 2000) |
|---|---|
| phenylalanyl chain | A polypeptide component of insulin containing 30 amino acyl residues, beginning with a phenylalanyl residue (NH2-terminus); insulin is formed by the linkage of a B chain to an A chain by two disulfide bonds; the amino-acid composition of the B chain is a function of species. Synonym: phenylalanyl chain. (05 Mar 2000) |
| closed chain compound | Any compound in which the constituent atoms, or any part of them, form a ring. Used mainly in organic chemistry where: 1) numerous compound's contain rings of carbon atoms (carbocyclic compound's) or carbon atoms plus one or more atoms of other types (heterocyclic compound's), usually nitrogen, oxygen, or sulfur; 2) where the atoms in the ring are all of the same element (homocyclic or isocyclic compound); 3) where the ring is saturated or contains nonconjugated double bonds (alicyclic compound), the compound is similar in properties to the corresponding acyclic compound (e.g., cyclohexane resembles hexane); 4) where the ring contains conjugated double bonds in a closed loop in which there are 4n + 2 (where n is an integer) delocalised π electrons (Huckel's rule) (aromatic compound; e.g., benzene, pyridine), it is more stable than the corresponding saturated ring and exhibits unusual chemical properties characteristic of itself and not of other types of rings or of acyclic compound's. These aromatic compounds have the ability to sustain an induced ring current. Synonym: closed chain compound, ring compound. (05 Mar 2000) |
| cold chain | A system of protection against high environmental temperatures for heat-labile vaccines, sera and other biological preparations. (05 Mar 2000) |
| P light chain | <protein> Myosin light chain that can be phosphorylated by myosin light chain kinase, as a result of phosphorylation, the myosin is activated. (18 Nov 1997) |
| corticosteroid side-chain-isomerase | <enzyme> Converts 11-deoxycorticosterone to 20-hydroxy-3-oxypregn-4-en-21-al; also acts as an epimerase at c-20 Registry number: EC 5.3.1.21 Synonym: corticosteroid side chain isomerase, ccsci (26 Jun 1999) |
| polymerase chain reaction | <molecular biology, technique> The first practical system for in vitro amplification of DNA and as such one of the most important recent developments in molecular biology. Two synthetic oligonucleotide primers, which are complementary to two regions of the target DNA (one for each strand) to be amplified, are added to the target DNA (that need not be pure), in the presence of excess deoxynucleotides and Taq polymerase, a heat stable DNA polymerase. In a series (typically 30) of temperature cycles, the target DNA is repeatedly denatured (around 90_C), annealed to the primers (typically at 50-60_C) and a daughter strand extended from the primers (72_C). As the daughter strands themselves act as templates for subsequent cycles, DNA fragments matching both primers are amplified exponentially, rather than linearly. The original DNA need thus be neither pure nor abundant and the polymerase chain reaction has accordingly become widely used not only in research, but in clinical diagnostics and forensic science. Acronym: PCR (14 Oct 1997) |
| myosin light chain | <protein> The light chains of the muscle protein myosin. Each molecule of myosin is composed of two heavy chains and two pairs of light chains. The light chains have a molecular weight of about 20 kD and there is one dissimilar pair of light chains associated with each heavy chain. The proteins all have sequence homology to calmodulin, but not all with calcium binding activity. Several types are known: regulatory light chains (LC 2, DNTB light chains) probably regulate the ATPase activity of the heavy chain directly (through the binding of calcium) or indirectly (activating when they themselves are phosphorylated by myosin light chain kinase) and essential light chains (LC 1, LC 3, alkali light chains), which have a more subtle and apparently nonessential role. In molluscan muscle the EDTA light chains (similar to LC 2 from vertebrate muscle) confer calcium sensitivity on the myosin itself. The light chains are "calmodulin-like" proteins that bind calcium. Two of them can be removed easily, and two with difficulty. The light chains bind the heavy chains in the vicinity of the head groups of the myosin. (12 Dec 1998) |
| myosin light chain kinase | <enzyme> An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and calmodulin. The 20-kD light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction. Chemical name: ATP:myosin-light-chain O-phosphotransferase Registry number: EC 2.7.1.117 (12 Dec 1998) |
| haemolytic chain | The haemolysis that occurs when complement is activated by the previously formed union of erythrocytes and specific antibody. (05 Mar 2000) |
| H chain | <protein> Heavy chain of immunoglobulin, see IgG, IgM, etc. (18 Nov 1997) |
| xenobiotic medium chain fatty acid - coenzyme A ligase | <enzyme> Partial amino acid sequence of enzyme from bovine liver mitochondria given I first source; has high sequence homology to human and rat sa protein Registry number: EC 6.2.1.- Synonym: xl-i ligase, xl-i carboxylic acid - CoA ligase (26 Jun 1999) |
| short chain | In bacteriology, a string of two to eight cells. (05 Mar 2000) |
| short-chain acyl-CoA dehydrogenase | See: acyl-CoA dehydrogenase (NADPH+). (05 Mar 2000) |
| short-chain beta-hydroxyacyl-CoA dehydrase | <enzyme> Forms trans-2-enoyl-CoA; maximal activity with trans-2-hexenoyl-CoA, followed by crotonyl-CoA; not the same as EC 4.2.1.17 Registry number: EC 4.2.1.- Synonym: beta-hydroxybutyryl-CoA dehydrase, short-chain beta-hydroxyacyl-coenzyme a dehydrase (26 Jun 1999) |
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