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"ACE : angiotensin converting enzyme"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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¿µ¹® angiotensin ÇÑ±Û ¾ÈÁö¿ÀÅÙ½Å
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  ÄáÆÏ¿¡¼­ ½ÅÀåÀÇ Ç÷·ù¿Í Ç÷¾ÐÀ» °¨ÁöÇϴ ¼¼Æ÷ÀΠġ¹Ð¹ÝÁ¡(macula densa)°ú Å丮°ç¼¼Æ÷(JG cell)¿¡¼­ Ç÷·ù¿Í Ç÷¾ÐÀÇ ÀúÇϰ¡ ÀÖÀ» °æ¿ì¿¡ ·¹´ÑÀ̶ó´Â ¹°ÁúÀÌ ºÐºñµÇ°Ô µÈ´Ù. ÀÌ ·¹´ÑÀ̶ó´Â ¹°ÁúÀº Ç÷Áß¿¡ Á¸ÀçÇϴ ¾ÈÁö¿ÀÅÙ½ÅÀ̶ó´Â ¹°ÁúÀ» ¾ÈÁö¿ÀÅٽŠIÀ¸·Î º¯È­½Ã۰í ÀÌ ¾ÈÁö¿ÀÅٽŠIÀ̶ó´Â ¹°ÁúÀº ¾ÈÁö¿ÀÅٽŠI Àüȯȿ¼Ò¿¡ ÀÇÇØ¼­ ¾ÈÁö¿ÀÅÙ½ÅII¶ó´Â ¹°Áú·Î µÈ´Ù. ¾ÈÁö¿ÀÅٽŰú ¾ÈÁö¿ÀÅٽŠIÀ̶ó´Â ¹°ÁúÀº ±× ÀÛ¿ëÀÌ °ÅÀÇ ¾øÁö¸¸ ¾ÈÁö¿ÀÅٽŠII¶ó´Â ¹°ÁúÀº °­·ÂÇϰԠÇ÷°ü¼öÃàÀ» ½Ã۰í À̷ΠÀÎÇØ¼­ Ç÷¾ÐÀÇ »ó½ÂÀ» °¡Á®¿À¸ç µ¿½Ã¿¡ ºÎ½ÅÀ» ÀÚ±ØÇÏ¿© ¾Ëµµ½ºÅ×·ÐÀ» ºÐºñÇϰԠÇÑ´Ù. ¾ÈÁö¿ÀÅÙ½ÅÀ̶õ Ç÷°üÀ» ¼öÃà½ÃŰ°í ¾Ëµµ½ºÅ×·ÐÀÇ ºÐºñ¸¦ À¯µµÇÔÀ¸·Î½á Ç÷¾ÐÀÇ »ó½ÂÀ» °¡Á®¿À´Â ¹°ÁúÀÌ´Ù. ±×¸®°í ±× ÀÛ¿ëÀº ·¹´Ñ-¾ÈÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ×·ÐÀ¸·Î À̾îÁö´Â Ã¼°è¿¡ ÀÇÇØ¼­ Á¶ÀýµÇ°í ÀÌ·ç¾îÁø´Ù.
¿µ¹® serum enzyme ÇÑ±Û Ç÷ûȿ¼Ò
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¿µ¹® enzyme ÇÑ±Û È¿¼Ò
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  »ý¹°Ã¼ ¼¼Æ÷¼Ó¿¡¼­ ÇÕ¼ºµÇ°í, ÁַΠ¼¼Æ÷³»¿¡¼­ ÁøÇàµÇ´Â È­ÇйÝÀÀÀ» Ã˸ÅÇϴ ´Ü¹éÁú·Î ½ÃÇè°ü³»¿¡¼­µµ °°Àº Ã˸ÅÀÛ¿ëÀ» ÇÑ´Ù. ÀÌ È¿¼Ò´Â ÀΰøÀûÀ¸·Î ¸¸µç ¾î¶² Ã˸ÅÁ¦º¸´Ù ±× Æ¯À̼º°ú Ã˸ÅÀÛ¿ëÀ̠Ź¿ùÇѠƯº°ÇÑ »ýüºÐÀÚÀÌ´Ù. ½ÅÁø´ë»ç, Áï ¼¼Æ÷³»¿¡¼­ ÀϾ´Â ¹°ÁúÀÇ È­ÇÐÀû º¯È¯Àº È¿¼ÒÀÇ ÀÛ¿ë¿¡ ÀÇÇØ ¸Å¿ì ºü¸£°í ¿øÇÒÇϰԠÀÌ·ç¾îÁø´Ù. À̰ÍÀº È¿¼ÒÀÇ Ã˸ŠȿÀ²ÀÌ ³ôÀº Á¡°ú È¿¼ÒÀÇ ±âÁú Æ¯À̼º ¶§¹®ÀÌ´Ù. È¿¼Ò¹ÝÀÀÀº »ó¿Â, »ó¾Ð, ÃÖÀû pH µî ÀûÀýÇÑ Á¶°Ç ¾Æ·¡¿¡¼­ ÁøÇàµÈ´Ù. ¶Ç È¿¼ÒÀÇ ÁÖü°¡ ´Ü¹éÁúÀ̱⠶§¹®¿¡ ´Ü¹éÁúÀ» º¯¼º½Ã۴ ¿­, °­»ê, °­¾ËÄ®¸®, À¯±â¿ë¸Å µî¿¡ ÀÇÇØ ±× ÀÛ¿ëÀ» ÀҴ´Ù. È¿¼Ò´Â »ýü¿¡ ³Î¸® ºÐÆ÷Çϸç, º¹ÀâÇÏ°í ´Ù¾çÇÑ ´ë»ç¹ÝÀÀÀ» Ã˸ÅÇϱ⠶§¹®¿¡ Á¾·ùµµ ¸¹´Ù. ¾Õ¼­ ¸»ÇÑ ¹Ù¿Í °°ÀÌ ´ëºÎºÐÀÇ È¿¼Ò´Â ¼¼Æ÷³»¿¡ Á¸ÀçÇÏÁö¸¸, Ç÷¾×°ú ±×¿ÜÀÇ °£Áú¾×¿¡ µé¾î Àֱ⵵ ÇÏ°í ¼ÒÈ­È¿¼Ò·ù󷳠ü¿Ü·Î ºÐºñµÇ´Â °Íµµ ÀÖ´Ù.
¿µ¹® enzyme-linked immunoabsorbent assay ÇÑ±Û È¿¼Ò¸é¿ªÃøÁ¤¹ý
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  È¿¼Ò°áÇո鿪ÈíÂøÁ¦ °ËÁ¤¹ýÀ¸·Î ¹ø¿ªµÇ°í ÀÖ´Ù. ÀÌ ¹ýÀº Ç׿ø(¶Ç´Â Ç×ü)¿¡ ¾ËÄ®¸® Æ÷½ºÆÄŸ¾ÆÁ¦ ¶Ç´Â Æä¸£¿Á½Ãµð¾ÆÁ¦ µîÀÇ »ê¼Ò¸¦ °áÇÕ½ÃÄÑ µÎ°í ±× »ê¼ÒȰ¼ºÀ» ÁöÇ¥·Î »ï¾Æ Ç׿øÇ×ü¹ÝÀÀÀÇ Á¤µµ¸¦ ¾È ´ÙÀ½ ¿©±â¿¡¼­ Ç׿ø(¶Ç´Â Ç×ü)ÀÇ ¾çÀ» ±¸Çϴ °ÍÀÌ´Ù. ÀÌ ¹ýÀÇ ÀÌÁ¡À¸·Î¼­ °í°¨µµ, Á¶ÀÛÀÇ °£´ÜÇÔ ¹× ¹æ»ç¼±¸é¿ªÃøÁ¤¹ýó·³ ¹æ»ç¼º¹°ÁúÀ» »ç¿ëÇÏÁö ¾Ê¾Æµµ µÈ´Ù´Â Á¡À» µé ¼ö ÀÖ´Ù. È£¸£¸óÀ̳ª ¸é¿ª±Û·ÎºÒ¸°ÀÇ Á¤·®¹ýÀ¸·Î¼­ ÀÀ¿ë µÇ°í ÀÖÀ¸¸ç ÃøÁ¤¿ë Å°Æ®µµ ½ÃÆÇµÇ°í ÀÌÀÖ´Ù.
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  • ¿µ¹®
    ÇѱÛ
  • angiotensin converting enzyme
    ¾ØÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • angiotensin converting enzyme inhibitor
    ¾ØÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò¾ïÁ¦Á¦
  • converting enzyme inhibitor
    Àüȯȿ¼Ò¾ïÁ¦Á¦
  • angiotensin
    ¾ØÁö¿ÀÅÙ½Å
  • renin-angiotensin-aldosterone system
    ·¹´Ñ-¾ØÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ׷аèÅë
  • antibody capture enzyme-linked immunosorbent assay
    Ç×üÆ÷ȹȿ¼Ò¸é¿ªÃøÁ¤(¹ý)
  • autolytic enzyme
    ÀÚ°¡¿ëÇØÈ¿¼Ò
  • adaptive enzyme
    ÀûÀÀÈ¿¼Ò
  • allosteric enzyme
    ¾Ë·Î½ºÅ׸®È¿¼Ò
  • blood enzyme level
    Ç÷ÁßÈ¿¼Ò³óµµ
  • brancher enzyme
    °¡ÁöÄ¡±âÈ¿¼Ò, ºÐÁöÈ¿¼Ò
  • branching enzyme
    °¡ÁöÄ¡±âÈ¿¼Ò, ºÐÁöÈ¿¼Ò
  • constitutive enzyme
    ±âº»±¸¼ºÈ¿¼Ò
  • cytosolic enzyme
    ¼¼Æ÷¾×È¿¼Ò
  • debrancher enzyme
    °¡ÁöÁ¦°ÅÈ¿¼Ò, Å»ºÐÁöÈ¿¼Ò
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 12 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • enzyme-linked immunosorbent assay
    È¿¼Ò¸é¿ªÃøÁ¤¹ý
  • enzyme
    È¿¼Ò
  • inhibitory enzyme
    ¾ïÁ¦È¿¼Ò
  • oxidative enzyme
    »êÈ­È¿¼Ò
  • proteolytic enzyme
    ´Ü¹éÁúºÐÇØÈ¿¼Ò
  • rate limiting enzyme
    ¼ÓµµÁ¶ÀýÈ¿¼Ò
  • redox enzyme
    »êȭȯ¿øÈ¿¼Ò
  • regulatory enzyme
    Á¶ÀýÈ¿¼Ò
  • respiratory enzyme
    È£ÈíÈ¿¼Ò
  • restriction enzyme
    Á¦ÇÑÈ¿¼Ò
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • converting enzyme inhibitor
    Àüȯȿ¼Ò¾ïÁ¦Á¦
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • adaptive enzyme
    ÀûÀÀÈ¿¼Ò
  • allosteric enzyme
    ¾Ë·Î½ºÅ׸®È¿¼Ò
  • antibody capture enzyme-linked immunosorbent assay
    Ç×üÆ÷ȹȿ¼Ò¸é¿ªÃøÁ¤¹ý
  • autolytic enzyme
    ÀÚ°¡¿ëÇØÈ¿¼Ò
  • double-sandwich enzyme-linked immunosorbent assay
    °ãÈ¿¼Ò¸é¿ªÃøÁ¤¹ý
  • enzyme activity
    È¿¼ÒȰ¼º, È¿¼ÒȰ¼ºµµ
  • enzyme assay
    È¿¼ÒÃøÁ¤
  • enzyme labeled antibody
    È¿¼ÒÇ¥ÁöÇ×ü
  • enzyme-linked immunosorbent assay
    È¿¼Ò¸é¿ªÃøÁ¤¹ý
  • blood enzyme level
    Ç÷ÁßÈ¿¼Ò³óµµ
  • branching enzyme
    °¡ÁöÄ¡±âÈ¿¼Ò, ºÐÁöÈ¿¼Ò
  • enzyme-linked immunoelectrotransfer blot
    È¿¼Ò¸é¿ªÀÌÀû¹ý, È¿¼Ò¿¬°ü¸é¿ªÀü±âÀü´ÞÁ¡
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • ACE : angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò.
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  • ¿µ¹®
    ÇѱÛ
  • ACE=> angiotensin converting enzyme
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò(ï®üµý£áÈ)
  • ACEI : angiotensin converting enzyme inhibitor
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò¾ïÁ¦Á¦(ï®ü½ý£áÈåäð¤ð¥).
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò.
  • angiotensin converting enzyme inbibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin converting enzyme inhibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin-converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • Converting enzyme
    Àüȯȿ¼Ò(ï®üµý£áÈ)
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • angiotensin ii
    ¾ÈÁö¿ÀÅÙ½ÅII
  • renin angiotensin aldosterone pressor
    ·¹´Ñ¾ÈÁö¿ÀÅٽž˵µ½ºÅ׷н ¾Ð°è(¡­ã°äâ
  • renin angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅٽŰè(¡­Í§).
  • renin-angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅÙ½Åü°è
  • renin-angiotensin system
    ·¹´Ñ-¾ÈÁö¿ÀÅٽŰè(¡­Ìõ)
  • renin-angiotensin-aldosterone axis
    ·¹´Ñ-¾ÈÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ×·ÐÃà<--°è>
  • renin-angiotensin-aldosterone system
    ·¹´Ñ-¾ÈÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ×·Ðü°è
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò.
  • angiotensin converting enzyme inbibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin converting enzyme inhibitor
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò ¾ïÁ¦¹°Áú<¾à>.
  • angiotensin-converting enzyme
    ¾ÈÁö¿ÀÅÙ½ÅÀüȯȿ¼Ò
  • converting enzyme inhibitor
    Àüȯȿ¼Ò¾ïÁ¦Á¦.
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • angiotensin ii
    ¾ÈÁö¿ÀÅÙ½ÅII
  • renin angiotensin aldosterone pressor
    ·¹´Ñ¾ÈÁö¿ÀÅٽž˵µ½ºÅ׷н ¾Ð°è(¡­ã°äâ
  • renin angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅٽŰè(¡­Í§).
  • renin-angiotensin system
    ·¹´Ñ¾ÈÁö¿ÀÅÙ½Åü°è
  • renin-angiotensin system
    ·¹´Ñ-¾ÈÁö¿ÀÅٽŰè(¡­Ìõ)
  • renin-angiotensin-aldosterone axis
    ·¹´Ñ-¾ÈÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ×·ÐÃà<--°è>
  • renin-angiotensin-aldosterone system
    ·¹´Ñ-¾ÈÁö¿ÀÅÙ½Å-¾Ëµµ½ºÅ×·Ðü°è
  • adaptive enzyme
    ÀûÀÀÈ¿¼Ò(îêëëý£áÈ).
  • allosteric enzyme
    ¾Ë·Î½ºÅ׸®È¿¼Ò(¡­ý£áÈ).
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • enzyme-linked immunoelectrotransfer blot (EITB)
    È¿¼Ò¸é¿ªÀÌÀû¹ý
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • converting enzyme
    "Àüȯ È¿¼Ò(ï®üµý£áÈ), (ÔÒ) serum converting enzyme"
  • serum converting enzyme
    Ç÷û Àüȯ È¿¼Ò(úìôèï®üµý£áÈ)
  • angiotensin I
    ¾ÈÁö¿ÀÅٽŠI
  • angiotensin II
    ¾ÈÁö¿ÀÅٽŠII
  • converting phage
    Àüȯ(ï®üµ) ÆäÀÌÁö
  • serum prothrombin converting factor
    Ç÷û(úìôè) ÇÁ·ÎÆ®·Òºó ÀüȯÀÎÀÚ(ï®üµì×í­)
  • activating enzyme
    "ºÎȰȿ¼Ò (Ý·üÀý£áÈ), Ȱ¼ºÈ­È¿¼Ò (üÀàõûùý£áÈ)"
  • acyl activating enzyme
    ¾Æ½ÇºÎȰȿ¼Ò (Ý·üÀý£áÈ)
  • acyl enzyme
    ¾Æ½ÇÈ¿¼Ò(ý£áÈ)
  • acyl enzyme intermediates
    ¾Æ½ÇÈ¿¼Ò Áß°£Ã¼(ñéÊàô÷)
  • adaptive enzyme
    ÀûÀÀÈ¿¼Ò(îêëëý£áÈ)
  • alteration enzyme
    º¯ÇüÈ¿¼Ò(ܨúþý£áÈ)
  • ambiquitous enzyme
    ¾çÁ¸È¿¼Ò(å»ðíý£áÈ)
  • amino acid activating enzyme
    ¾Æ¹Ì³ë»ê(ß«) Ȱ¼ºÈ­(üÀàõûù) È¿¼Ò(ý£áÈ)
  • amplifier enzyme
    ÁõÆøÈ¿¼Ò(ñòøëý£áÈ)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
  • ELISA [=enzyme-linked immunosorbent assay]
    ELIZA, ¿¤¸®ÀÚ
  • enzyme
    È¿¼Ò
  • enzyme-linked immunosorbent assay [=ELISA]
    ELISA, ¿¤¸®ÀÚ
  • proteolytic enzyme
    ´Ü¹éÁúºÐÇØÈ¿¼Ò
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
ACE Angiotensin Converting Enzyme
  = Kininase II
  = Dipeptidyl Carboxypepti...
ACE acetonitrile; acetylcholine esterase; acute cerebral encephalopathy; acute coronary event; adrenocor...
PACE Pacing and Clinical Electrophysiology; paired basic amino acid cleaving enzyme; personalized aerobic...
ACEDS angiotensin-converting enzyme dysfunction syndrome
ACEI angiotensin-converting enzyme inhibitor
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
ACE ANGIOTENSIN CONVERTING ENZYME
ACE Angiotensin converting enzyme activity
ACE inhibitor angiotensin converting enzyme inhibitor
ACE angiotensin I converting enzyme gene
ACE ANG I converting enzyme
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • angiotensin converting enzyme
    ¾ÈÁö¿ÀÅٽŠÀüȯ È¿¼Ò
  • angiotensin-converting enzyme
    ¾ÈÁö¿ÀÅٽŠÀüȯ È¿¼Ò
  • converting enzyme
    Àüȯ È¿¼Ò
  • ACE
    ¾ÈÁö¿ÀÅٽŠÀüȯȿ¼Ò
    angiotensin converting enzymeÀÇ ¾àÀÚ.
  • angiotensin
    ¾ÈÁö¿ÀÅÙ½Å
    1. °­·ÂÇÑ Ç÷°ü ¼öÃà ÀÛ¿ë°ú ºÎ½Å ÇÇÁú¿¡¼­ÀÇ ¾Ëµµ½ºÅ×·Ð »ýÇÕ¼º ¹× ºÐºñ ÃËÁøÀÛ¿ëÀÌ ÀÖ´Ù. ºÐÀÚ·®À» ±âÁØÀ¸·Î ³ë¿¡Çdz×ÇÁ¸°¿¡ ºñÇØ ¾à 40¹è³ª °­ÇÑ Ç÷¾Ð »ó½Â È¿°ú¸¦ °¡Áö°í ÀÖ´Ù. 2. Ç÷¾×¿¡ Á¸ÀçÇÏ´Â Æú¸® ÆéŸÀ̵å·Î¼­ Ç÷ÀåÀÇ ·¹´Ñ°ú Ç÷û a2 ±Û·ÎºÒ¸°¿¡ ÀÇÇÏ¿© Çü¼ºµÈ´Ù. deca
  • angiotensin I
    ¾ÈÁö¿ÀÅٽŠI
    ºÒȰ¼ºÇüÀ¸·Î ÆéŸÀÌµå ºÐÇØ È¿¼ÒÀÇ ÀÛ¿ë¿¡ ÀÇÇÏ¿© ¿ÁŸÆéŸÀ̵åÀÇ ¾ÈÁö¿ÀÅٽŠ¥±·Î ÀüȯµÈ´Ù. À̰ÍÀÌ °­·ÂÇÑ Ç÷°ü ¼öÃà ¹°ÁúÀÌ¸ç ¶ÇÇÑ ºÎ½Å ÇÇÁú¿¡¼­ ¾Ëµµ½ºÅ×·Ð ºÐºñ ÃËÁø ¹°ÁúÀ̱⵵ ÇÏ´Ù.
  • digestive enzyme
    ¼ÒÈ­ È¿¼Ò
  • enzyme activator
    È¿¼Ò Ȱ¼ºÁ¦
  • enzyme disorder
    È¿¼Ò Àå¾Ö
  • enzyme immunoassay
    È¿¼Ò ¸é¿ª ÃøÁ¤¹ý
    ¼Ò·®ÀÌ¶óµµ ±× Ȱ¼ºÀ» °ËÃâÇÒ ¼ö ÀÖ´Â °í°¨µµÀÇ È¿¼Ò¸¦ Ç¥½ÃÀÚ·Î Çϰí Ç׿ø ȤÀº Ç×ü, ³ª¾Æ°¡¼­´Â ƯÀÌÀûÀ¸·Î ¹ÝÀÀÇÏ´Â ¹°Áú, lectin, C1q µîÀ» È­ÇÐÀûÀ¸·Î °áÇÕ½ÃÄÑ, Ç׿ø ȤÀº Ç×ü µûÀ§¸¦ ÃøÁ¤ÇÏ´Â ¹æ¹ýÀÌ´Ù.
  • enzyme inhibition
    È¿¼Ò ¾ïÁ¦
  • enzyme labeled antibody
    È¿¼Ò Ç¥Áö Ç×ü
  • enzyme marker study
    È¿¼Ò Ç¥Áö ¿¬±¸
  • enzyme precursor
    È¿¼Ò Àü±¸Ã¼
  • enzyme-labelled antibody
    È¿¼Ò Ç¥Áö Ç×ü
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angiotensin-converting enzyme <enzyme> This hydrolase enzyme cleaves the decapeptide angiotensin I (biologically inactive) to form active angiotensin II by angiotensin-converting enzyme which removes a dipeptide (histidylleucine) from angiotensin I.
Angiotensin II causes contraction of vascular smooth muscle and thus raises blood pressure and stimulates aldosterone release from the adrenal glands. Angiotensin is finally broken down by angiotensinases.
Elevations in angiotensin converting enzyme are seen sarcoidosis, histoplasmosis, alcoholic cirrhosis, asbestosis, berylliosis, diabetes, Hodgkin's disease, hyperthyroidism, amyloidosis, primary biliary cirrhosis, idiopathic pulmonary fibrosis, pulmonary embolism, scleroderma, silicosis, tuberculosis, Gaucher's disease and leprosy. The normal values are 18 to 67 U/ml over 20 years of age (people under 20 have higher levels).
Drugs that inhibit ACE are used to treat hypertension and congestive heart failure.
See: angiotensin-converting enzyme inhibitor
Acronym: ACE
(12 Aug 2000)
angiotensin-converting enzyme inhibitor <pharmacology> A class of drugs used in the treatment of hypertension and heart failure.
They exert their haemodynamic effect mainly by inhibiting the renin-angiotensin system and produce a reduction of peripheral arterial resistance. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.
(14 Aug 2000)
angiotensin-converting enzyme secretase <enzyme> Converts ace from a membrane-bound to a soluble form; not inhibited by thiol, serine or acid enzyme inhibitor but is inhibited by edta and 1,10-phenanthroline
Registry number: EC 3.4.99.-
Synonym: ace secretase
(26 Jun 1999)
interleukin-1 converting enzyme <biochemistry> Cytoplasmic cysteine protease that is uniquely responsible for cleaving proIL-1_ (31 or 33 kD) into mature IL-1_ (17.5 kD), the active cytokine is then released by a nonstandard mechanism (there is no signal sequence and it does not pass through the Golgi).
The enzyme seems to be composed of two nonidentical subunits derived from a single proenzyme. The ICE gene has some homology with the ced 9 gene of C. Elegans, the product of which is involved in mediating cell death by apoptosis.
(11 Mar 1998)
ACE <enzyme> This hydrolase enzyme cleaves the decapeptide angiotensin I (biologically inactive) to form active angiotensin II by angiotensin-converting enzyme which removes a dipeptide (histidylleucine) from angiotensin I.
Angiotensin II causes contraction of vascular smooth muscle and thus raises blood pressure and stimulates aldosterone release from the adrenal glands. Angiotensin is finally broken down by angiotensinases.
Elevations in angiotensin converting enzyme are seen sarcoidosis, histoplasmosis, alcoholic cirrhosis, asbestosis, berylliosis, diabetes, Hodgkin's disease, hyperthyroidism, amyloidosis, primary biliary cirrhosis, idiopathic pulmonary fibrosis, pulmonary embolism, scleroderma, silicosis, tuberculosis, Gaucher's disease and leprosy. The normal values are 18 to 67 U/ml over 20 years of age (people under 20 have higher levels).
Drugs that inhibit ACE are used to treat hypertension and congestive heart failure.
See: angiotensin-converting enzyme inhibitor
Acronym: ACE
(12 Aug 2000)
ACE inhibitor <pharmacology> A group of antihypertensive medications that work by inhibiting an enzyme (angiotensin-converting enzyme) that is important in the regulation of blood pressure.
Studies have also indicated that it may help prevent or slow the progression of kidney disease in patients with diabetes.
Examples include: captopril, ramipril, enalapril, losartan potassium, bepridil and lisinopril.
(12 Mar 1998)
ACE level <investigation> This is a blood test which measures the concentration of angiotensin-converting enzyme (ACE) in the bloodstream.
Elevations in angiotensin-converting enzyme are seen sarcoidosis, histoplasmosis, alcoholic cirrhosis, asbestosis, berylliosis, diabetes, Hodgkin's disease, hyperthyroidism, amyloidosis, primary biliary cirrhosis, idiopathic pulmonary fibrosis, pulmonary embolism, scleroderma, silicosis, tuberculosis, Gaucher's disease and leprosy.
The normal values are 18 to 67 U/ml over 20 years of age (people under 20 have higher levels).
(15 Jan 1998)
medication, ace-inhibitor Agents that inhibit ACE (angiotensin-converting enzyme), thereby acting as vasodilators (really as anti-vasoconstrictors), lightening the stress load on the heart.
(12 Dec 1998)
vasopressin-converting aminopeptidase <enzyme> Activity found in brain which converts vasopressin into centrally active metabolites
Registry number: EC 3.4.11.-
Synonym: vp-c aminopeptidase
(26 Jun 1999)
dynorphin-converting endopeptidase <enzyme> Enzyme from human cerebrospinal fluid; cleaves dynorphin a and b and neoendorphin at the arg(6)-arg(7) or arg(6)-lys(7) bonds
Registry number: EC 3.4.21.-
Synonym: dynorphin-neo-endorphin endopeptidase, dc-endopeptidase
(26 Jun 1999)
urokinase-converting protease <enzyme> Degrades synthetic urokinase substrates and stimulates urokinase
Registry number: EC 3.4.21.-
Synonym: urokinase cofactor
(26 Jun 1999)
angiotensin <hormone> A family of oligopeptides ranging in size from angiotensin precursors with 14 amino acids to the active vasoconstrictor angiotensin II with 8 amino acids, or their analogs or derivatives.
The amino acid content varies with the species and changes in that content produce antagonistic or inactive compounds.
Angiotensinogen (renin substrate) is a 60 kD polypeptide released from the liver and cleaved in the circulation by renin to form the biologically inactive decapeptide angiotensin I. This is in turn cleaved to form active angiotensin II by Angiotensin-converting Enzyme (ACE). Angiotensin II causes contraction of vascular smooth muscle and thus raises blood pressure and stimulates aldosterone release from the adrenal glands. Angiotensin is finally broken down by angiotensinases.
(12 Aug 2000)
angiotensin amide <chemical> 1-l-asparagine-5-l-valine-angiotensin II. The octapeptide amide of bovine angiotensin II used to increase blood pressure by vasoconstriction.
Pharmacological action: vasoconstrictor agents.
Chemical name: Angiotensin II, 1-L-asparagine-5-L-valine-
(12 Dec 1998)
angiotensin I <chemical> The decapeptide precursor of angiotensin II, generated by the action of renin on angiotensinogen. It has limited pharmacologic activity.
Chemical name: Angiotensin I
(12 Dec 1998)
angiotensin II <chemical> The active form of angiotensin. An octapeptide found in blood, it is synthesised from angiotensin I and quickly destroyed. Angiotensin II causes profound vasoconstriction with resulting increase in blood pressure. The clinically and experimentally used bovine form has valine in position 5 where the human form has isoleucine.
Pharmacological action: vasoconstrictor agents.
Chemical name: Angiotensin II
(12 Dec 1998)
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