| ¿µ¹® | lymphatic system | ÇÑ±Û | ¸²ÇÁ°è |
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| ¼³¸í | ´ë°³ ¸Æ°ü°è¶ó°í Çϸé, Ç÷°ü°è¿Í ¸²ÇÁ°ü°è¸¦ ÇÕÃļ ¸»ÇÑ´Ù. ÀÌÁß¿¡ ¸²ÇÁ¿¡ ÀÇÇØ ÀÌ·ç¾îÁö´Â ÇϳªÀÇ °èÅëÀÌ´Ù. |
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| ¿µ¹® | immune system | ÇÑ±Û | ¸é¿ªÃ¼°è |
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| ¿µ¹® | urinary system | ÇÑ±Û | ºñ´¢±â°èÅë |
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| ¼³¸í | ºñ´¢±â°èÅëÀ̶óÇϸé ÄáÆÏÀ¸·ÎºÎÅÍ ½ÃÀÛÇØ¼ ¿ä°ü, ¹æ±¤, ¿äµµ¿¡ À̸£´Â ÀÏ·ÃÀÇ ¿ÀÁÜ»ý¼º ¹× ÀúÀå, ¹è¼³±â°üÀ» ÀÏÄ´´Ù. ÄáÆÏÀº ±æÀÌ ¾à 2.5cm, Æø ¾à 5.1cm, µÎ²² ¾à 2.5cm, ¹«°Ô ¾à 120~160gmÀ¸·Î¼, ³»Ãø¿¡ ÄáÆÏ¹®ÀÌ ÀÖ¾î Ç÷°ü, ½Å°æ, ¿ä°üÀÌ ÃâÀÔÇϰí ÀÖ´Ù. ÄáÆÏÀº ¼ÓÁú°ú °ÑÁú·Î ÀÌ·ç¾îÁ® ÀÖÀ¸¸ç ¼öÁúÀº 10~15°³ÀÇ Ãßü(¿ÀÁÜÀ» ¸ðÀ¸´Â ¿ªÇÒ)¸¦ Çü¼ºÇÏ°í °ÑÁúÀº ¾à 100¸¸°³ÀÇ ÄáÆÏ´ÜÀ§À¸·Î ±¸¼ºµÇ¾î ÀÖ´Ù. ¿ä¼¼°üÀº Å丮ÂÊ´¢¼¼°ü, Çî·¹°í¸®, ¸ÕÂÊ´¢¼¼°ü, ÁýÇÕ°üÀ¸·Î Çü¼ºµÇ¾î ÀÖÀ¸¸ç, Ãßü¿Í ¼úÀÜ, ±ò¶§±â¸¦ °ÅÃÄ ¿ä°üÀ¸·Î ¿¬°áµÈ´Ù. ÄáÆÏÀº Ç÷¾×À» ¿©°úÇÏ¿© ½Åü ½ÅÁø´ë»çÀÇ ÃÖÁ¾»ê¹°À» ¿ÀÁÜÀÇ ÇüÅ·Π¹è¼³Çϸç, ¼¼Æ÷¿Ü¾×(extracellular fluid)ÀÇ ÀüÇØÁú³óµµ¸¦ Á¶ÀýÇÑ´Ù. ÄáÆÏ¿¡¼ Çü¼ºµÈ ¿ÀÁÜ´Â ¿ä°üÀ» °ÅÃÄ ¹æ±¤¿¡¼ ÀúÀåµÇ°í ÀÖ´Ù°¡ Àû´çÇÑ ½Ã±â°¡ µÇ¸é ¿äµµ¸¦ ÅëÇØ ¿Ü°è·Î ¹èÃâµÈ´Ù. |
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| ¿µ¹® | reproductive system | ÇÑ±Û | »ý½Ä±â°èÅë |
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| ¼³¸í | 1.³²¼º»ý½Ä°èÅë: ³²¼º»ý½Ä±â´Â Á¤ÀÚ(sperm)¸¦ »ý¼ºÇÏ´Â °íȯ°ú Á¤ÀÚÀÇ ¼º¼÷, ¿î¹Ý, ±×¸®°í »çÁ¤¿¡ °ü¿©ÇÏ´Â ºÎ°íȯ, Á¤°ü, À½°æ(penis) µîÀ¸·Î ÀÌ·ç¾îÁ® ÀÖÀ¸¸ç, ºÎ¼Ó±â°üÀ¸·Î ¿ÜºÐºñ»ùÀÎ Á¤³¶(seminal vesicle), Àü¸³»ù(prostate), ¿äµµ¸Á¹°»ù(bulbourethral gland, Cowper¡¯s gland) µîÀ» °®Ãß°í ÀÖ´Ù. °íȯÀº Á¤ÀÚ¸¦ »ý»êÇÏ´Â »ý½Ä»ùÀÎ µ¿½Ã¿¡ ³²¼ºÈ£¸£¸ó(testosterone)À» ºÐºñÇÏ´Â ³»ºÐºñ»ùÀÌ´Ù. °íȯ¿¡¼ ºÐºñµÇ´Â ³²¼ºÈ£¸£¸óÀº Á¤ÀÚ»ý¼º°ú »ý½Ä±âÀÇ ¹ß´Þ ¹× À¯Áö¿¡ ÇʼöÀûÀÎ ¿ªÇÒÀ» ÇϹǷΠ³²¼º»ý½Ä±â´ÉÀÇ ¿øÃµÀº °íȯ¿¡ ÀÖ´Ù°í º¼ ¼ö ÀÖ´Ù. 2.¿©¼º»ý½Ä°èÅë: ¿©¼º»ý½Ä±â´Â ³ÀÚ¸¦ »ý¼ºÇÏ´Â ³¼Ò¿Í ³ÀÚ¸¦ ÀÚ±ÃÀ¸·Î ¿î¹ÝÇÏ´Â ³°ü, ±×¸®°í Àڱðú Áú·Î ÀÌ·ç¾îÁ® ÀÖÀ¸¸ç ¿ÜºÐºñ¼±ÀÎ ¹Ù¸£Å縰»ù¸¦ °®Ãß°í ÀÖ´Ù. ³¼Ò´Â ³ÀÚ¸¦ »ý¼ºÇÏ´Â »ý½Ä»ùÀÎ µ¿½Ã¿¡ ¿©¼ºÈ£¸£¸óÀ» ºÐºñÄÉÇÏ´Â ³»ºÐºñ»ùÀÌ´Ù. ¿ù°æÁÖ±â Àü¹ÝºÎ¿¡ ³ÀÚ¸¦ »ý¼º½Ã۱âÀ§ÇØ ¼º¼÷µÇ°í ÀÖ´Â ³Æ÷¿¡¼ ºÐºñµÇ´Â ¿¡½ºÆ®·Î°ÕÀº ¿©¼º 2Â÷ ¼ºÂ¡ÀÇ ¹ß´ÞÀ» °üÀåÇÒ »Ó ¾Æ´Ï¶ó Àڱ󻸷À» ÀåÂ÷ ¼öÁ¤µÉ ¼öÁ¤¶õÀÌ Âø»óÇϱ⿡ ¾Ë¸ÂÀº »óÅ·Π¸¸µé¾îÁØ´Ù. ³ÀÚ°¡ ºÐºñµÇ°í ³²Àº Ȳü¿¡¼ ºÐºñµÇ´Â Ǫ·Î°Ô½ºÅ×·ÐÀº Àڱ󻸷À» º×µµ·Ï ÇÏ¸é ºÐºñ¾×À» Áõ°¡½Ã۸ç ÀڱñÙÀÇ ¼öÃàÀ» ¹æÇØÇÏ¿© ÀӽŽà ÀÓ½ÅÀ» Áö¼Ó½ÃŰ´Â ¿ªÇÒÀ» ÇÑ´Ù. |
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| benzylamine oxidase | <enzyme> An aspect of monoamine oxidase, catalyses the oxidation of benzylamine to form benzaldehyde, ammonia and hydrogen peroxide. Registry number: EC 1.4.3.- (12 Dec 1998) |
|---|---|
| beta-aminoisobutyric acid oxidase | <enzyme> Fad-stimulated, probably forms methylmalonylsaemialdehyde Registry number: EC 1.4.3.- Synonym: baib-oxidase (26 Jun 1999) |
| branched chain acyl-CoA oxidase | <enzyme> Enzyme from human liver peroxisomes acts on both 2-methyl branched fatty acyl- and bile acid-CoA intermediates, unlike rat liver peroxisomes which have separate enzymes for branched chain fatty acids (pristanoyl-CoA) and bile acid-CoA; involved in beta-oxidation of fatty acids and bil Registry number: EC 1.3.3.- Synonym: 2-methyl-branched chain acyl-CoA oxidase, hbrcacox (26 Jun 1999) |
| galactose oxidase | <enzyme> An enzyme that oxidises galactose in the presence of molecular oxygen to d-galacto-hexodialdose. It is a copper protein. Chemical name: D-Galactose:oxygen 6-oxidoreductase Registry number: EC 1.1.3.9 (12 Dec 1998) |
| vanillyl-alcohol oxidase | <enzyme> From penicillium simplicissimum; contains fad; forms vanillin or 4-hydroxybenzaldehyde, respectively, from vanillyl alcohol or 4-hydroxybenzyl alcohol Registry number: EC 1.1.3.- Synonym: 4-hydroxybenzyl alcohol oxidase (26 Jun 1999) |
| palmitoyl CoA oxidase | <enzyme> In peroxisomes; forms hydrogen peroxide Registry number: EC 1.3.3.- Synonym: palmityl CoA oxidase, palmitoyl coenzyme a oxidase (26 Jun 1999) |
| malate oxidase | <enzyme> Fad-dependent Registry number: EC 1.1.3.3 (26 Jun 1999) |
| veratryl alcohol oxidase | <enzyme> From pleurotus sajor-caju (polyporaceae); converts veratryl alcohol and various aromatic alcohols to aldehydes, reducing o2 to h2o2 Registry number: EC 1.1.3.- Synonym: veratryl alcohol oxidase I, veratryl alcohol oxidase II (26 Jun 1999) |
| carotene oxidase | <enzyme> Enzyme that catalyses the oxidative conversion of arachidonic acid to the hydroxyeicosenoic acid (HETE) structure in the synthesis of leucotrienes. (18 Nov 1997) |
| gibberellin 7-oxidase | <enzyme> A 2-oxoglutarate-dependent dioxygenase from pumpkin endosperm, involved in gibberellin biosynthesis; 314 amino acids, mw 35.7 kD; genbank u61386 Registry number: EC 1.14.11.- Synonym: ga 7-oxidase, ga-7-dioxygenase (26 Jun 1999) |
| catechol oxidase | <enzyme> An enzyme of the oxidoreductase class that catalyses the reaction between catechol and oxygen to yield benzoquinone and water. It is a complex of copper-containing proteins that acts also on a variety of substituted catechols. Chemical name: 1,2-Benzenediol:oxygen oxidoreductase Registry number: EC 1.10.3.1 (12 Dec 1998) |
| cellobiose oxidase | <enzyme> Haem-containing flavoprotein, requires molecular oxygen Registry number: EC 1.1.3.- (26 Jun 1999) |
| glucooligosaccharide oxidase | <enzyme> Oxidises oligosaccharides with glucose on the reducing end and each sugar residue joined by an alpha- or beta-1,4 glucosidic bond; active on maltose, lactose, cellobiose and maltose derivatives up to seven residues Registry number: EC 1.1.3.- (26 Jun 1999) |
| glucose oxidase | <enzyme> An enzyme which converts glucose into gluconic acid and hydrogen peroxide (H2O2). It is used to help diagnose diabetes by determining if glucose is present in the patients urine, if the glucose is present, the hydrogen peroxide produced in the reaction can be detected by reacting it with an indicator to change the colour of the urine. (09 Oct 1997) |
| glucose oxidase method | <chemical pathology> A highly specific method for measurement of glucose in serum or plasma by reaction with glucose oxidase, in which gluconic acid and hydrogen peroxide are formed. (05 Mar 2000) |
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