米氏常數 的英文怎麼說
中文拼音 [mǐshìchángshǔ]
米氏常數
英文
km-
A novel catalytic property of hemin is described. in ammonium buffer medium of ph 8. 08. 9, hemin has an ability to catalyze the decoloration of bromopyro - gallol red. oxygen dissolved in solution plays a role as an oxidant in the reaction. with sodium dodecylbenzenesulfonate and ethanol as effect - enhancing agents, the catalytic system obeys the michaelis - menten equation of enzymatic catalysis. the michaelis constant, catalytic constant and specificity constant of the system are estimated by lineweaver - burk plot to be 3. 710
在ph 8 . 08 . 9氨性緩沖介質中， hemin催化溶解氧氧化溴鄰苯三酚紅的褪色反應。在sdbs和30 %乙醇的增效作用下，催化體系服從michaelis - menten方程。用lineweaver - burk作圖法求得米氏常數催化常數和專一性常數分別為3 . 7103. 2. 1. 4 ) which was prepared by precipitation of the water extract of the culture of aspergillus niger with ammonium sulfate and desalted by sephadex g - 25, and was further fractionated by two steps of deae - toyopearl 650m and one step of poros 20pi chromatography. the other was a p - glucosidase ( ec. 3. 2. 1. 21 ) which was prepared by the above g - 25 fractions and was further fractionated by two steps of deae - toyopearl 650m chromatography. the specific activity of the endoglucanase with sodium carboxymethyl cellulose was estimated to be 433. 38 hj / mg
-葡萄糖苷酶對水楊素的比活力為597 . 12iu mg ，並對其專一，不能水解棉花和羧甲基纖維素鈉；分子量為117 . 5kda ，加dtt後分子量不變；該組分最適ph和溫度分別為4 . 5和70 ，在ph5 . 0 、 50下對水楊素鈉的米氏常數km為3 . 73mg ml ，最大反應速度vm為0 . 088mg葡萄糖（ ml ? min ） ；與文獻中從黑麴黴中分離的-葡萄糖苷酶比較后發現，該組分是一個新的-葡萄糖苷酶。It was found that the composite film containing 28. 6 % polyisoprene suited well for biosensor construction. the apparent michaelis constanst and activation energy for the immobilized glucose oxidase are 11. 9 mm and 41. 1 kj - mol " 1, respectively. the biosensor response was influenced by ph value of determined solution, applied potential and operational temperature
研究發現，復合膜中聚異戊二烯含量28 . 6為傳感器製作的最佳條件；固定化葡萄糖氧化酶的表觀米氏常數為11 . 9mm ，酶催化反應的表觀活化能為41 . 1kj ? mol ~ （ - 1 ） ；被測溶液的ph值、工作電位、使用溫度等對葡萄糖傳感器的響應有一定的影響。The study on the kinetics of the enzyme showed that the enzymatic reaction with lactic acetate as the substrate accorded with the michaelis - menten equation. it michaelis constant km was 5. 77, and the maximum velocity was 0. 45 u mol / l min
酶動力學研究表明：該酯酶在以乳酸乙酯為底物的酶促反應符合米氏方程，米氏常數為km ： 5 . 77 ，最大反應速度vmax為： 0 . 45 mol l ? min 。The optimum temperature, the ph and storage stability were 80 ?, 8. 0 and 28 days respectively. the reclaimed efficiency of immobilized enzyme that is prepared by this vector is over 76 %, the michaelis - menten kinetic constants were evaluated for the immobilized and the freely soluble enzymes, they were 21. 64147 and 7
固定化酶的最適反應溫度是80 ，最適ph是8 . 0 ，操作半衰期是28天，固定化酶的酶活回收率在76 %以上，通過米氏方程測定了固定化酶和溶液酶的米氏常數，分別為21 . 64147和7 . 0836 。分享友人