½ðÄê»á¡¤(jinnianhui)½ð×ÖÕÐÅÆ³ÏÐÅÖÁÉÏ-Gold Annual Meeting

  • <½ðÄê»á¡¤(jinnianhui)½ð×ÖÕÐÅÆ³ÏÐÅÖÁÉÏ-Gold Annual Meetingva class='nhiomg'>
    <½ðÄê»á¡¤(jinnianhui)½ð×ÖÕÐÅÆ³ÏÐÅÖÁÉÏ-Gold Annual Meeting class='trbtsx'>
    »¶Ó­À´µ½ÉϺ£½ðÄê»á¡¤(jinnianhui)½ð×ÖÕÐÅÆ³ÏÐÅÖÁÉÏ-Gold Annual Meeting£¡

    021-54888888/15800441009

    Æ·Öʱ£Ö¤ ¡¤ ½ðÄê»á¡¤(jinnianhui)½ð×ÖÕÐÅÆ³ÏÐÅÖÁÉÏ-Gold Annual MeetingÊÔ¼Á

    µ±Ç°Î»ÖÃ: Ê×Ò³ > ¿ÆÑвúÆ· > Éú»¯ÊÔ¼Á > øÀà > µ°°×øS

    ²úÆ·ÖÐÐÄ

    • µ°°×øS

      ¹æ¸ñ£º
      ÊýÁ¿£º

      ¹ºÂòÊýÁ¿

      ¼Û¸ñ£º£¤
      • Æ·ÅÆ : ½ðÄê»á¡¤(jinnianhui)½ð×ÖÕÐÅÆ³ÏÐÅÖÁÉÏ-Gold Annual MeetingÉúÎï
      • Ŀ¼ºÅ : TW26049
      • Ó¦Óà : ½ö¹©¿ÆÑÐʹÓÃ
      • ±£´æÌõ¼þ : 2¡«8¡æ
      • »õÆÚ : ÏÖ»õ
      • ÉÌÆ·¿â´æ£º80
    • ÉÌÆ·ÏêÇé
    • ²Î¿¼ÎÄÏ×
    • ˵Ã÷ÊéÏÂÔØ
    • ÉÌÆ·ÆÀÂÛ0
    • Ïà¹Ø²úÆ·

    ÖÐÎÄÃû³Æ £º µ°°×øS


    ÆäËûÖÐÎÄÃû³Æ £º V8µ°°×øS


    Ó¢ÎÄÃû³Æ £º Protease S Aureus


    ÆäËûÓ¢ÎÄÃû³Æ £º Endoproteinase Glu-C from Staphylococcus aureus V8£»V8 Protease


    C A S £º 66676-43-5


    ¼¶ ±ð £º BR


    À´ Ô´ £º Staph aureus V8


    Activity £º ¡Ý500units/mg


    »îÁ¦¶¨Òå £º One Unit causes a change of 0.001 A280 nm per minute at 37¡æ, pH 7.8 using casein as the substrate


    ²úÆ·ÃèÊö £º Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27,000 daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO- and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau (Methods Enzymol., 45, 469, 1976).


    ÐÔ ×´ £º ·ÛÄ©¡£


    Óà ; £º Éú»¯Ñо¿¡£


    ±£ ´æ £º 2¡«8¡æ


    ¡¾ÍøÕ¾µØÍ¼¡¿¡¾sitemap¡¿
    ¡¾ÍøÕ¾µØÍ¼¡¿¡¾sitemap¡¿