| ¿µ¹® | venereal disease, sexually transmitted diseases | ÇÑ±Û | ¼ºº´ |
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| ¼³¸í | º¸ÆíÀûÀ¸·Î ¼º±³ ¶Ç´Â ¼º±âÁ¢ÃË¿¡ ÀÇÇØ °É¸®´Â Á¢ÃË Àü¿°º´À¸·Î ¸Åµ¶, ÀÓÁú, ¹«¸¥±Ë¾ç, »ô±¼À°¾ÆÁ¾ µîÀ» ¸»ÇÑ´Ù. Ä¡·á´Â ¿øÀαտ¡ µû¸¥ ÀûÀýÇÑ Ç×»ý¿ä¹ýÀÌ´Ù. |
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| ¿µ¹® | VDRL(venereal disease research laboratory) | ÇÑ±Û | ¼ºº´ ¿¬±¸½ÇÇè½Ç |
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| ¼³¸í | ¸Åµ¶±ÕÀÇ reagin¿¡ ´ëÇÑ Ç×ü. ¸Åµ¶ÀÇ ¼±º°°Ë»ç·Î »ç¿ëµÇ¸ç ¸Åµ¶ Ä¡·á¿¡ ´ëÇÑ ¹ÝÀÀ ¿©ºÎ¿Í Ä¡·áÈ¿°ú ÆÇÁ¤¿¡µµ »ç¿ëµÈ´Ù. ¸Åµ¶¿Ü¿¡µµ Àü½Å¼ºÈ«¹Ý¼º³¶Ã¢, ·ù¸¶Æ¼½º°üÀý¿° µî¿¡¼µµ ¾ç¼ºÀ¸·Î ³ªÅ¸³¯ ¼ö ÀÖ´Ù. |
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| ¿µ¹® | hemolytic disease of newborn | ÇÑ±Û | ½Å»ý¾Æ¿ëÇ÷º´ |
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| ¼³¸í | ½Å»ý¾Æ¿¡¼ ÀûÇ÷±¸°¡ ºñÁ¤»óÀûÀ¸·Î ¸¹ÀÌ ÆÄ±«µÇ´Â º´À¸·Î žÆÀû¸ð±¸Áõ(erythroblastosis fetalis)¿Í °°Àº ¶æÀ¸·Î ¾²ÀδÙ. À̰ÍÀº ¾î¸Ó´Ï¿¡°Ô¼ »ý»êµÈ ½Å»ý¾Æ³ª žÆÀÇ ÀûÇ÷±¸¿¡ ´ëÇÑ Ç×ü°¡ ŹÝÀ» °Ç³Ê¿Í¼ žÆÀÇ ÀûÇ÷±¸¿Í °áÇÕÇÏ¿©¼ »ý±â´Â ¿ëÇ÷¼ººóÇ÷À» À̸£´Â ¸». Áï ½Å»ý¾Æ³ª žÆÀÇ ÀûÇ÷±¸ÀÇ Ç×ü°¡ ¾î¸Ó´ÏÀÇ ¸ö¿¡¼ »ý»êÀÌ µÇ°í À̰ÍÀÌ Å¹ÝÀ» ÅëÇØ¼ žƿ¡°Ô ³Ñ¾î°¡¼ žÆÀÇ ÀûÇ÷±¸¿Í °áÇÕÀ» Çϰí ÀÌ Ç×ü¿Í °áÇÕÇÑ ÀûÇ÷±¸´Â ÆÄ±«°¡ µÇ¾î¼ ºóÇ÷ÀÌ »ý±ä °ÍÀ» žÆÀû¸ð±¸ÁõÀ̶ó°í ÇÑ´Ù. À̰ÍÀº Rh Àû¸ð±¸Áõ(Rh erythroblastosis)¿Í ABO Àû¸ð±¸Áõ(ABO erythroblastosis)·Î ³ª´ ¼ö°¡ ÀÖ´Ù. |
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| ¿µ¹® | coronary artery disease | ÇÑ±Û | ½ÉÀ嵿¸Æº´ |
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| ¼³¸í | ½ÉÀ嵿¸ÆÀ̶õ ½ÉÀå¿¡ Ç÷¾×À» °ø±ÞÇÏ´Â µ¿¸ÆÀ» ¸»ÇÑ´Ù. ½ÉÀåµµ ´Ù¸¥ ±ÙÀ°°ú ¸¶Âù°¡Áö·Î Ç÷¾×À» °ø±Þ¹Þ¾Æ¾ß ¼öÃàÀ» ÇÒ ¼ö°¡ ÀÖ´Â ±â°üÀ¸·Î ½ÉÀåÀÇ Ç÷¾×À» °ø±ÞÇÏ´Â µ¿¸ÆÀ» ½ÉÀ嵿¸ÆÀ̶ó°í ÇÑ´Ù. ½ÉÀ嵿¸Æº´À̶õ ½ÉÀ嵿¸ÆÀÇ ³»°æÀÌ Á¼¾ÆÁ®¼ »ý±â´Â ÁúȯÀ¸·Î ÇãÇ÷½ÉÀ庴(ischemic heart disease)À̶ó°íµµ ºÒ¸°´Ù. °ü»óµ¿¸ÆÀÌ Á¼¾ÆÁú °æ¿ì¿¡´Â ½ÉÀåÀ¸·Î °¡´Â Ç÷¾×ÀÇ ¾çÀÌ Àû¾îÁ®¼ ½ÉÀå¿¡ ÃæºÐÇÑ Ç÷¾×ÀÌ °ø±ÞÀÌ µÇÁö ¸øÇϹǷΠ¿©·¯ °¡Áö º´ÀûÀÎ Çö»óÀÌ »ý±ä´Ù. ½ÉÀ嵿¸ÆÀÌ Á¼¾ÆÁö´Â µ¥¿¡´Â ¿©·¯ °¡Áö ¿øÀÎÀÌ ÀÖÀ» ¼ö°¡ ÀÖÀ¸³ª ÁÖ·Î ½ÉÀ嵿¸ÆÀÇ µ¿¸Æ°æÈÁõ¿¡ ÀÇÇÑ´Ù. µ¿¸Æ°æÈÁõÀ̶õ µ¿¸ÆÀÇ ³»Ãþ¿¡ Áö¹æ°ú ÄÝ·¹½ºÅ×·Ñ·Î ÀÌ·ç¾îÁø Á×Á¾(atheroma)°¡ »ý±â´Â ÁúȯÀ¸·Î Á×Á¾ÀÌ »ý±ä µ¿¸ÆÀº Á×Á¾ÀÌ Ç÷°üÀÇ ³»ºÎ·Î µ¹ÃâÇÏ°Ô µÇ¾î¼ Ç÷°üÀÇ ³»°æÀÌ ÀÛ¾ÆÁö°Ô µÈ´Ù. ½ÉÀ嵿¸Æº´Àº ±× Á¤µµ¿¡ µû¶ó¼ Çù½ÉÁõ(angina pectoris)¿Í ½É±Ù°æ»öÁõ(myocardial infarction)À¸·Î ³ª´«´Ù. Çù½ÉÁõÀº ½ÉÀ嵿¸ÆÀÇ ºÎºÐÀû Æó¼â¿¡ ÀÇÇØ¼ Æò»ó½Ã¿¡´Â Áõ»óÀÌ ¾øÁö¸¸ ½ÉÀåÀÌ ¸¹Àº Ȱµ¿À» ÇÒ °æ¿ì¿¡ ½ÉÀå¿¡ Çǰ¡ ÃæºÐÇÑ ¸¸Å °ø±ÞÀÌ µÇÁö ¾Ê¾Æ¼ »ý±â´Â Áúº´À¸·Î Æò»ó½Ã¿¡ ½¯ °æ¿ì¿¡´Â ¾Æ¹« Áõ»óÀÌ ¾øÁö¸¸ ¿îµ¿À̳ª °ú½Ä µîÀÇ ¿øÀÎÀ¸·Î ½ÉÀåÀÌ ¸¹Àº ¿îµ¿À» ÇÒ °æ¿ì¿¡ ½ÉÀå¿¡ °ø±ÞµÇ´Â Ç÷¾×ÀÇ ¾çÀÌ ¸ðÀÚ¶ó¼ Áõ»ó(´ë°³ °¡½¿ºÎÀ§¿¡ Áã¾îÂ¥´Â µíÇÑ ÅëÁõ)ÀÌ »ý±ä´Ù. ½É±Ù°æ»öÁõÀ̶õ ½ÉÀ嵿¸ÆÀÇ ¿ÏÀüÆó¼â¿¡ ÀÇÇØ¼ ½ÉÀåÀÇ ±ÙÀ°ÀÌ Ç÷¾×À» ÀüÇô °ø±Þ¹ÞÁö ¸øÇؼ ½ÉÀåÀÇ ±ÙÀ°ÀÌ ½â´Â °æ¿ì¸¦ ¸»ÇÑ´Ù. |
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| ¿µ¹® | heart disease | ÇÑ±Û | ½ÉÀ庴 |
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| ¼³¸í | ¼øÈ¯±â Áúȯ Áß ½ÉÀåÀÇ º´. ÀϹÝÀûÀ¸·Î ½ÉÀåÇ÷°üÀ̳ª ½ÉÀåÀÇ º´µµ Æ÷ÇԵȴÙ. º´ÅÍÀÇ ºÎÀ§¿¡ ÀÇÇÑ º´¸®ÇغÎÇÐÀû ºÐ·ù¿Í º´Àο¡ ÀÇÇÑ ºÐ·ù°¡ ÀÖ´Ù. ÀüÀÚ´Â ¼ö ½Ê ³â ÀüºÎÅÍ ¾²¿©Á® ¿ÔÀ¸³ª ±Ù³â¿¡ ¿Í¼ º»ÁúÀûÀÎ ¿øÀοä¹ýÀÌ °¡´ÉÇÏ°Ô µÈ ÀÌÈÄ´Â ÈÄÀÚÀÇ ºÐ·ù°¡ ÀÇÀǰ¡ ÀÖ¾î¼ ¸¹ÀÌ ¾²ÀÌ°Ô µÇ¾ú´Ù. º´ÅÍ ºÎÀ§·Î´Â ½É³»¸·(ÆÇ¸·)-½ÉÀå±Ù-½ÉÀ帷, ±× ¹ÛÀÇ °ÍÀ» µé ¼ö ÀÖÀ¸¸ç, °¢°¢ ½É³»¸·¿°-½ÉÀåÆÇ¸·Áõ-½É±Ù¿°-½É±Ù°æ»ö-½ÉÀ帷¿°-¼±Ãµ¼º ½ÉÀ庴(½ÉÀå±âÇü) µîÀÌÆ÷ÇԵȴÙ. º´Àκ°¿¡¼´Â ½ÉÀå±âÇüÀ» ºñ·ÔÇÏ¿© ·ù¸¶Ä¡½º ½ÉÀ庴-¸Åµ¶¼º ½ÉÀ庴-°íÇ÷¾Ð¼º ½ÉÀ庴-½ÉÀ嵿¸Æ°æÈ¼º ½ÉÀ庴-Æó¼º½ÉÀå-¼¼±Õ¼º ½É³»¸·¿°-½ÉÀå½Å°æÁõ µîÀ¸·Î ³ª´©¾îÁö¸ç, ºÎÁ¤¸ÆÀ̳ª ¹æ½ÇÂ÷´Ü µîÀÇ ÀÚ±ØÀüµµ°èÀÇ Àå¾Ö¿¡ ÀÇÇÑ °Íµµ Áõ¼¼ÀÇ Çϳª·Î º¼ ¼ö ÀÖ´Ù. ½ÉÀ庴Àº ÀÚ°¢ÀûÀ¸·Î´Â ¹«Áõ¼¼ÀÎ °Í¿¡¼ºÎÅÍ ½ÉÀå±â´É»ó½Ç·Î È£Èí°ï¶õ±îÁö ÀÖ´Ù. |
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| LC | Laennec cirrhosis; Langerhans cell; late clamped; large chromophobe; lecithin cholesterol acyltransf... |
|---|---|
| VH | variable domain of heavy chain; variable heavy chain |
| VL | variable domain of the light chain; variable light chain |
| ECG | Electro-Cardio-Graphy(-Gram); ½ÉÀüµµ = EKG 1. Conducting System Structu... |
| AHD | acquired hepatocerebral degeneration; acute heart disease; antihyaluronidase; antihypertensive drug;... |
| 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) |
| MyoD heavy chain kinase | <enzyme> Required for actin activation of the magnesium atpase activity of dictyostelium myosin id (myod); specific for myod Registry number: EC 2.7.1.- Synonym: 110-kD protein kinase, dictyostelium, dictyostelium 110-kD protein (26 Jun 1999) |
| myosin heavy chain | <protein> See myosin: do not confuse with heavy meromyosin which is a subfragment of the heavy chain of myosin II. (18 Nov 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) |
| heavy chain | <protein> In general, the larger polypeptide in a multimeric protein. Thus the immunoglobulin heavy chain is of 50 kD, the light chain of 22 kD, whereas in myosin the heavy chain is very much larger (220 kD) than the light chains (~20 kD). (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) |
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