| ¿µ¹® | Raynaud disease | ÇÑ±Û | ·¹À̳뺴 |
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| ¼³¸í | ±â´ÉÀû Ç÷°ü °æ·ÃÀ» ÀÏÀ¸Å°´Â º´À¸·Î °Ç°ÇÑ ÀþÀº ¿©¼ºÀÇ ÆÈ´Ù¸® ÀÛÀº µ¿¸ÆÀ» ħ¹üÇÑ´Ù. ÇÁ¶û½º ÀÇ»ç M.·¹À̳ë(1834~1881)°¡ º¸°íÇÑ °ÍÀ¸·Î ÀÌ º´Àº ÁÖ·Î ¼Õ°¡¶ô, ¼Õ, ¶§·Î´Â ÄÚ³¡À̳ª ¹ßµî, ¸öÀÇ ¸»´ÜºÎ ¼Òµ¿¸ÆÀ» ħ¹üÇÑ´Ù. Çѳðú °¨Á¤Àڱؿ¡ ÀÇÇÏ¸ç ¼Õ°¡¶ôÀº ¹é»öÀ¸·Î ´ÙÀ½Àº û»öÀ¸·Î, ±×¸®°í Àû»öÀ¸·Î º¯ÇÑ´Ù. ¿©¼º¿¡°Ô È£¹ßÇÑ´Ù. |
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| ¿µ¹® | rheumatic heart disease | ÇÑ±Û | ·ù¸¶Æ¼½º½ÉÀ庴 |
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| ¼³¸í | »ç½½¾Ë±Õ°¨¿° ÈÄ »ý±â´Â ½ÉÀåÆÇ¸·º´ÀÌ´Ù. ¿øÀÎÀº A±º -¿ëÇ÷»ç½½¾Ë¿¡ ÀÇÇÑ Àεο°ÈÄ ÀÏÁ¾ÀÇ ¸é¿ª¹ÝÀÀÀ¸·Î ¹ßº´ÇÑ´Ù. Áø´ÜÀº Á¸ÀÇ ±âÁØ¿¡ ÀÇÇÑ´Ù. (1) ÁÖ¿ä±âÁØÀº °üÀý¿° ½ÉÀå¿°(½ÉÀåºñ´ë, ½ÉÀåÀâÀ½, ½ÉÀå±â´É»ó½Ç µî) ¹«µµÁõ: ¹«´çÀÌ ÃãÀ» Ãß´Â °Í °°Àº ÇൿÀÇ ¹ßÀÛÁõ¼¼. ¿¬º¯È«¹Ý: »¡°£ Å׵θ®¸¦ °¡Áø ÇǺκ´º¯Àº ÇÇÇϰáÀý(subcutaneous nodule): ÇǺΠ¹Ø¿¡ »ý±ä °áÀý, (2)Âü°í ±âÁØÀº ¿, °üÀýÅë, EKG»ó PR¿¬Àå: ½ÉÀüµµ ¼Ò°ß ±Þ¼º±â ¹ÝÀÀ¹°Áú(¿¹: ESR, CRP)ÀÇ »ó½Â, ·ù¸¶Æ¼½º¿ Ä¡·á´Â Æä´Ï½Ç¸°À¸·Î Ä¡·áÇÏ°í ½ÉÀåÀÇ ÈÄÀ¯Áõ ¶ÇÇÑ Æä´Ï½Ç¸°À¸·Î ¿¹¹æÇÑ´Ù. |
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| ¿µ¹® | chronic obstructive pulmonary disease | ÇÑ±Û | ¸¸¼ºÆó¼âÆóº´ |
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| ¼³¸í | ¸¸¼ºÀûÀ¸·Î ±âµµÀÇ Æó¼â¸¦ °¡Á®¿À´Â º´À» À̸£´Â ¸». ´ë°³ ¸¸¼º±â°üÁö¿°, ±â°üÁö õ½Ä, Æó±âÁ¾ÀÇ 3°¡Áö º´À» ¸»ÇÑ´Ù. ¸¸¼º±â°üÁö¿°À̶õ ±â°üÁöÀÇ ¸¸¼º¿°ÁõÀ» ¸»ÇÑ´Ù. ±â°üÁöÀÇ ¿°ÁõÀ¸·Î ÀÎÇØ¼ ±â°üÁöÀÇ Á¡¸·¿¡ ºÎÁ¾ÀÌ »ý±â°í ÀÌ·Î ÀÎÇØ¼ ±â°üÁöÀÇ ³»°æÀÌ Á¼¾ÆÁ®¼ ±âµµÀÇ Æó¼â¸¦ °¡Á®¿Â´Ù. ´ë°³ Èí¿¬°ú ¹ÐÁ¢ÇÑ ¿¬°üÀ» °¡Áö¸ç, È£Èí°ï¶õ, ±âħ, ±×¸®°í °¡·¡(´ë°³ »öÀÌ Çª¸£°í Á¡µµ°¡ ³ôÀº °¡·¡)°¡ Áõ»óÀ¸·Î ³ªÅ¸³´Ù. Æó±âÁ¾Àº ±â°üÁöÀÇ º®À» ÁöÁöÇÏ´Â Á¶Á÷ÀÇ ÆÄ±«¿¡ ÀÇÇØ¼ ±â°üÁö°¡ Á¦ ¸ð¾çÀ» °®ÃßÁö ¸øÇÏ°í ¹«³ÊÁö°Ô µÇ¾î ±âµµÀÇ Æó¼â°¡ ÀϾ´Â º´ÀÌ´Ù. Áï ±â°üÁö°¡ °ü ¸ð¾çÀ¸·Î ÆØÆØÇÏ°Ô ÆìÁö´Â °ÍÀ» ÁöÁöÇÏ´Â Á¶Á÷ÀÇ ÆÄ±«¿¡ ÀÇÇØ¼ °ü¸ð¾çÀ¸·Î ÆìÁöÁö ¸øÇØ °á±¹Àº ÆóÆ÷³»¿¡ °ø±â°¡ Â÷°í ÆóÆ÷º®ÀÌ ÆÄ¿µÇ°í ±â°üÁö°¡ Á¼¾ÆÁö°Ô µÇ´Â º´À» ¸»ÇÑ´Ù. ±â°üÁöõ½ÄÀ̶õ ¿©·¯ °¡Áö Àڱؿ¡ ´ëÇØ¼ ±â°üÁö°¡ °ú¹ÎÇÑ ¹ÝÀÀÀ» º¸¿©¼ »ý±â´Â ±â°üÁöÀÇ °¡¿ªÀûÀÎ Æó¼â¸¦ ÀǹÌÇÑ´Ù. Áï Á¤»óÀο¡°Ô¼´Â ±â°üÁöÀÇ Æó¼â¸¦ º¸ÀÌÁö ¾Ê´Â Àڱؿ¡ ´ëÇØ¼ ±â°üÁöÀÇ Æó¼â°¡ »ý±â°í ±× ÀÚ±ØÀÌ ¾øÀ» °æ¿ì¿¡´Â ±â°üÁöÀÇ Æó¼â°¡ ¾ø¾îÁö´Â º´À» ¸»ÇÑ´Ù. |
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| ¿µ¹® | Buerger disease | ÇÑ±Û | ¹ö°Åº´ |
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| ¼³¸í | ¸»ÃÊ µ¿¸Æ°ú Á¤¸Æ¿¡ ¿°ÁõÀ» ÀÏÀ¸Å°´Â º´. ûÀå³âÃþÀÇ ³²ÀÚ¿¡°Ô Àß °É¸®´Â ´Ù¸® µ¿¸Æ¿¡ »ý±â´Â º´À¸·Î µ¿¸ÆÀÌ ¸·È÷°í ÅëÁõ ¶§¹®¿¡ ¹ßÀ» Àý±âµµ Çϴµ¥ ¿øÀÎÀº ¾Ë·ÁÁ® ÀÖÁö ¾Ê´Ù. º´¸íÀº ÀÌ º´À» ÃÖÃÊ·Î »ó¼¼ÇÏ°Ô º¸°íÇÑ ¹Ì±¹ÀÇ ÀÇ»ç L. ¹ö°Å(1879~1943)ÀÇ À̸§¿¡¼ ¿¬À¯ÇÑ´Ù. µ¿¾çÀο¡°Ô ¸¹Àº º´À¸·Î, ´ëºÎºÐ ÀþÀº ³²¼º, ƯÈ÷ Àå³â±â ³²¼º¿¡°Ô¼ ³ªÅ¸³´Ù. ¿øÀÎÀº ¾Ë ¼ö ¾øÀ¸³ª Èí¿¬ÀÌ º´ÀÇ ¾Çȸ¦ ÃÊ·¡ÇÑ´Ù. »çÁöÀÇ µ¿¸Æ°ú Á¤¸Æ¿¡ ¿°ÁõÀÌ ÀϾ Ç÷ÀüÀÌ »ý±â¸é ³»°À» ¸·¾Æ Ç÷¾×ÀÌ È帣Áö ¸øÇÏ°Ô µÇ¾î ±× ¾ÕÀÇ ¸»ÃÊÁ¶Á÷ÀÌ ±«»ç¿¡ ºüÁö°Å³ª ¼Õ¹ßÀÌ Â÷°©°í, ¼Õ°¡¶ô-¹ß°¡¶ôÀÌ º¸¶ó»ö ¶Ç´Â °ËÀº»öÀ¸·Î º¯ÇÑ´Ù. ¶Ç, ÀÌ Áõ¼¼°¡ °è¼ÓµÇ´Â µ¿¾È ¼Õ¹ß°¡¶ô¿¡ ÅëÁõÀÌ ÀϾ°í ±Ë¾çÀÌ ¹ß»ýÇÑ´Ù. Ä¡·á´Â Áõ¼¼ÀÇ Á¤µµ¿Í Æó»öµÈ Ç÷°üÀÇ ºÎÀ§¿¡ µû¶ó ¿¬°í¸¦ ¹Ù¸£°Å³ª Ç÷°üÈ®ÀåÁ¦-¼øÈ¯°³¼±Á¦-Ç÷¼ÒÆÇÀÀÁý¾ïÁ¦Á¦¸¦ »ç¿ëÇϳª, ¾î¶² Ä¡·áµµ È¿°ú°¡ ¾øÀ» °æ¿ì ¼Õ¹ß°¡¶ôÀÇ ¼ÒÀý´Ü, µå¹°°Ô´Â ¹«¸ ÀÌÇÏÀÇ ´ëÀý´ÜÀ» ÇØ¾ß ÇÑ´Ù. ÀϹÝÀûÀ¸·Î ÀÌ º´ÀÇ ¿¹ÈÄ´Â ¾çÈ£ÇÏ¿© Ç÷·ù°¡ ȸº¹µÇ°í ±Ë¾ç¸¸ Ä¡·áµÇ¸é Àç¹ßÀÌ Àû´Ù. |
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| ¿µ¹® | Behcet disease | ÇÑ±Û | º£Ã¼Æ®º´ |
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| ¼³¸í | ½ÉÇÑ Æ÷µµ¸·¿°, ¸Á¸·Ç÷°ü¿°, ½Ã°¢½Å°æÀ§Ãà, ±¸°-¼º±âÀÇ ¾ÆÇÁŸ¼º ±Ë¾ç, ±¤¹üÀ§ÇÑ Ç÷°ü¿°ÀÇ Â¡ÈÄ¿Í Áõ»óÀ» ³ªÅ¸³½´Ù. ¿øÀκҸíÀÇ Èñ±ÍÇÑ º´À¸·Î ÀþÀº ³²ÀÚ¿¡°Ô Àß ¹ß»ýÇÑ´Ù. |
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| HD | Haab-Dimmer [syndrome]; Hajna-Damon [broth]; Hansen disease; hearing distance; heart disease; helix ... |
|---|---|
| DDD | AV universal [pacemaker]; defined daily dose; degenerative disc disease; dehydroxydinaphthyl disulfi... |
| AD | accident dispensary; acetate dialysis; active disease; acute dermatomyositis; addict, addiction; ade... |
| PD | Doctor of Pharmacy; Dublin Pharmacopoeia; interpupillary distance; Paget disease; pancreatic duct; p... |
| RD | radial deviation; radiology department; rate difference; Raynaud disease; reaction of degeneration; ... |
| ribulose-1,5-bisphosphate carboxylase-oxygenase large subunit epsilonN-methyltransferase | <enzyme> An aspect of EC 2.1.1.43; trimethylates lys-14 of rubisco Registry number: EC 2.1.1.- Synonym: rubisco lsmt, rubisco large subunit lysine n-methyltransferase (26 Jun 1999) |
|---|---|
| ribulose bisphosphate carboxylase | <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis. Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants. In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen. Also called Fraction 1 protein, the major protein of leaves. Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing) Registry number: EC 4.1.1.39 (12 Dec 1998) |
| ribulosebisphosphate carboxylase-oxygenase activase | <chemical> Requires ATP; amino acid sequence given in first source Synonym: rubisco activase, rca protein (26 Jun 1999) |
| ribulose diphosphate carboxylase | <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis. Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants. In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen. Also called Fraction 1 protein, the major protein of leaves. Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing) Registry number: EC 4.1.1.39 (12 Dec 1998) |
| RuDP carboxylase | <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis. Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants. In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen. Also called Fraction 1 protein, the major protein of leaves. Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing) Registry number: EC 4.1.1.39 (12 Dec 1998) |
| phosphoenolpyruvate carboxylase | <enzyme> An enzyme with high affinity for carbon dioxide. It catalyses irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. Chemical name: Orthophosphate:oxaloacetate carboxy-lyase (phosphorylating) Registry number: EC 4.1.1.31 (12 Dec 1998) |
| phosphoenolpyruvate carboxylase kinase | <enzyme> From bryophyllum fedtschenkoi plant and maise; phosphorylates phosphoenolpyruvate carboxylase on serine near the n-terminus; activity controlled by circadian rhythms Registry number: EC 2.7.10.- Synonym: pep carboxylase kinase, pepc kinase (26 Jun 1999) |
| polyprenyl-4-hydroxybenzoate carboxylase | <enzyme> Involved in polyprenylphenol synthesis; implicated in flagellation of salmonella typhimurium Registry number: EC 4.1.1.- Synonym: ppphb carboxylase, polyprenyl-p-hydroxybenzoate carboxylase (26 Jun 1999) |
| preprothrombin carboxylase | <enzyme> Vitamin k-dependent, membrane-bound Registry number: EC 4.1.1.- (26 Jun 1999) |
| propionyl-CoA carboxylase | <enzyme> See also propionyl CoA carboxylase (ATP-hydrolyzing) (EC 6.4.1.4) Registry number: EC 4.1.1.41 Synonym: methylmalonyl-CoA decarboxylase, propionyl-coenzyme a carboxylase (26 Jun 1999) |
| pyruvic-malic carboxylase | <enzyme> An enzyme that catalyses the conversion of (s)-malate and NAD+ to oxaloacetate and NADH. Chemical name: (S)-Malate:NAD+ oxidoreductase Registry number: EC 1.1.1.37 (12 Dec 1998) |
| oxalosuccinic carboxylase | <enzyme> An enzyme of the oxidoreductase class that catalyses the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires magnesium, mn2+; it is activated by ADP, citrate, and calcium, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (the NADP+ enzyme is EC 1.1.1.42.) Chemical name: Isocitrate:NAD+ oxidoreductase (decarboxylating) Registry number: EC 1.1.1.41 (12 Dec 1998) |
| antibody deficiency disease | <syndrome> Any of a group of disorders associated with a defective antibody production due to defects in the B-type lymphocyte system or in T-type lymphocytes; chief manifestation is an increased susceptibility to infection by various microorganisms. See: agammaglobulinaemia, hypogammaglobulinaemia, immunodeficiency. Synonym: antibody deficiency disease. (05 Mar 2000) |
| deficiency disease | Any disease resulting from undernutrition or an inadequacy of calories, proteins, essential amino acids, fatty acids, vitamins, or trace minerals. (05 Mar 2000) |
| thrombotic disease due to protein c deficiency | Protein C is a protein in plasma that enters into the cascade of biochemical events leading to the formation of a clot. Deficiency of protein c results in thrombotic (clotting) disease and excess platelets with recurrent thrombophlebitis (inflammation of the vein that occurs when a clot forms). The clot can break loose and travel through the blood stream (thromboembolism) to the lungs causing a pulmonary embolism, brain causing a stroke (cerebrovascular accident), heart causing an early heart attack, skin causing what in the newborn is called neonatal purpura fulminans, the adrenal gland causing haemorrhage with abdominal pain, abnormally low blood pressure (hypotension), and salt loss. Protein c deficiency is due to possession of one gene (heterozygosity) in chromosome band 2q13-14. The possession of two such genes (homozygosity) is usually lethal. (12 Dec 1998) |
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