¿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» ÁßÈ­½ÃŲ´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 ÇÑ´Ù

Ȳ 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]