Hint | Food | ¸À°úÇâ | Diet | Health | ºÒ·®Áö½Ä | ÀÚ¿¬°úÇÐ | My Book | À¯Æ©ºê | Frims | ¿ø ·á | Á¦ Ç° | Update | Site |
¿ø·á ¡í ¹Ì³×¶ö ¡í È¿¼ÒÀÇ Á¾·ù ¹Ì³×¶ö : ¸ô¸®ºêµ§ Mo ÇÔÀ¯È¿¼Ò ¹Ì³×¶ö - öFe, ±¸¸®Cu, ¸Á°£Mn,¾Æ¿¬ Zn - Å©·Ò Cr, ¸ô¸®ºêµ§Mo, ¼¿·¹´Ï¿ò Se È¿¼ÒÀÇ Á¾·ù, ¹Ì³×¶ö - Fe ÇÔÀ¯ È¿¼Ò - Zn ÇÔÀ¯ È¿¼Ò - Mn ÇÔÀ¯ È¿¼Ò - Cu ÇÔÀ¯ È¿¼Ò - Se ÇÔÀ¯ È¿¼Ò - Mo ÇÔÀ¯ È¿¼Ò - Cr ÇÔÀ¯ È¿¼Ò - Xanthine oxidase´Â »êƾÀ» ¿ä»êÀ¸·Î ´ë»ç½ÃÄÑ ¼Òº¯À¸·Î ¹è¼³½ÃŲ´Ù ¿ä»êÀº Åëdz¼º °üÀý¿°À» À¯¹ßÇϱ⠶§¹®¿¡ ºÎÁ¤Àû ¹°Áú·Î °£ÁֵȴÙ. ±×·¯³ª ƯÁ¤ ¼öÁØ¿¡¼ ¿ä»êÀº °·ÂÇÑ Ç×»êÈÁ¦À̸ç ÇÁ¸®¶óµðÄ®À» ÁßȽÃŲ´Ù. ¸ô¸®ºêµ§Àº Áß¿äÇÑ Ç×»êÈÁ¦ ±â´É Á¶ÀýÀ» µ½´Â´Ù. Xanthine oxidase ¿ä»ê : Åëdz°ú °á¼® - Sulfite oxidase´Â À¯È² ÇÔÀ¯ ¾Æ¹Ì³ë»ê ´ë»çÀÇ ¸¶Áö¸· ´Ü°è¸¦ Ã˸ÅÇÑ´Ù. Sulfite(½Å°æ°è µ¶¼º ¹°Áú)¸¦sulfate·Î Àüȯ½ÃÄÑ ¹è¼³ÄÉ ÇѴ٠Ȳ Sulfur - ȲÇÔÀ¯ ¿µ¾ç¼ººÐ - DMSO, MSM, NAC, ½Ã½ºÆ¾ - Aldehyde oxidase´Â ¾Ëµ¥ÇÏÀ̵带 »êÀ¸·Î Àüȯ½ÃŲ´Ù AO is very similar in amino acid sequence to xanthine oxidase (XO). The active sites of AO has been found to have a superimposed structure to that of XO, in studies involving mouse liver. AO is a homodimer, and requires FAD, molybdenum (MoCo) and two 2FE-2S clusters as cofactors. These two 2FE-2S cofactors each bind to the two distinct 150-kDa monomers of AO. Three separate domains harbor these three requirements. There is a 20 kDa N-terminal which binds to the two 2FE-2S cofactors, a 40 kDa domain which provides a means of binding to the FAD, and a C-terminal which houses the molybdenum.[4] |
||||
|
|
|||