摘要
通过对酪氨酸酶催化底物L-DOPA反应速率的观察测定,研究了氨基葡萄糖(G-NH2)对酪氨酸酶的抑制作用。在反应液中加入50μL浓度为2.2 mg/mL G-NH2时(体系中G-NH2终浓度为36μg/mL),酶抑制率为50%。GNH2对酪氨酸酶的抑制作用是个复杂的过程,酶反应呈先促进后抑制。分析酶抑制曲线Lineweaver-Burk双倒数图,得出G-NH2为混合抑制剂,进一步研究发现多巴醌生产量会减少,抑制类型是不可逆抑制。
To study the inhibition effect of glucosamine( G-NH2) on tyrosinase,enzymatic reaction rate of L-DOPA was measured. The inhibition of enzyme was 50% when 50 μL G-NH2 was added to the reaction solution at a concentration of 2. 2 mg /mL( final concentration is 36 μg /mL). G-NH2 inhibition on tyrosinase was a complex process,and the enzyme reaction was increased before decreasing.By analyzing Lineweaver-Burk double reciprocal plot of enzyme inhibition,it showed that G-NH2 was a mixed inhibitor. Further studies found that dopaquinone reduced,which demonstrated that this inhibition was an irreversible inhibition.
出处
《生物学杂志》
CAS
CSCD
2014年第4期99-102,共4页
Journal of Biology
基金
宁波市科技计划项目(2006B100069)