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形式
lyophilized powder
质量水平
比活
100-300 units/mg protein
分子量
~175 kDa
组成
Protein, 65-85%
异质活性
Creatinase and urease ≤1%
Hexokinase and ATPase ≤0.1%
储存温度
2-8°C
应用
在临床分析中,该酶可与肌酸酶、肌氨酸脱氢酶或肌氨酸氧化酶以及甲醛脱氢酶结合用于酶法测定肌酐。
来自微生物的肌酐酶可通过与其他酶共固定进行肌酐测定而用于安培生物传感器的制备。
生化/生理作用
来自假单胞菌属的肌酐酶是一种每个亚基分子量为28.4 kDa的同六聚体酶。它是一种环状酰胺水解酶,可催化肌酸酐向肌酸的可逆性转化。每个单体在β-链的C末端和主要α-螺旋的N末端附近都含有一个双核锌中心。这些锌离子指示着活性位点的位置。
物理属性
等电点: 4.7
米氏常数:3.2 x 10‾2M(肌苷),5.7 x 10‾2M(肌酸)
结构:每摩尔的酶6个亚基(每个亚基结合一摩尔的锌)
抑制剂:Ag+、Hg++、N-溴代琥珀酰亚胺、EDTA
最适pH值: 6.5 − 7.5
最适温度: 70°C
pH稳定性: pH 7.5 − 9.0 (5°C,16小时)
热稳定性: 低于70°C(pH 7.5,30分钟)
米氏常数:3.2 x 10‾2M(肌苷),5.7 x 10‾2M(肌酸)
结构:每摩尔的酶6个亚基(每个亚基结合一摩尔的锌)
抑制剂:Ag+、Hg++、N-溴代琥珀酰亚胺、EDTA
最适pH值: 6.5 − 7.5
最适温度: 70°C
pH稳定性: pH 7.5 − 9.0 (5°C,16小时)
热稳定性: 低于70°C(pH 7.5,30分钟)
单位定义
在pH 8.0、25℃条件下,一个单位将在每分钟内水解1.0 mmole的肌苷
外形
含有蔗糖和BSA作为稳定剂的冻干粉末
分析说明
通过缩二脲法测定的蛋白质。
警示用语:
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
含少量动物源组分生物产品
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The reaction mechanism of creatinine-creatininase binding to form creatine as a final product has been investigated by using a combined ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics (MD) simulations. In MD simulations, an X-ray crystal structure of
The Annals of thoracic surgery, 91(2), 534-540 (2011-01-25)
Leukocyte filtration has been reported to reduce inflammatory damage during cardiopulmonary bypass. We evaluated the role of leukocyte filtration on hospital outcome and postoperative morbidity. Eighty-two consecutive patients who underwent isolated coronary artery bypass grafting were randomly assigned (1:1) to
Journal of molecular biology, 396(4), 1081-1096 (2010-01-02)
Creatininase is a binuclear zinc enzyme and catalyzes the reversible conversion of creatinine to creatine. It exhibits an open-closed conformational change upon substrate binding, and the differences in the conformations of Tyr121, Trp154, and the loop region containing Trp174 were
Journal of molecular biology, 337(2), 399-416 (2004-03-09)
Creatininase from Pseudomonas putida is a member of the urease-related amidohydrolase superfamily. The crystal structure of the Mn-activated enzyme has been solved by the single isomorphous replacement method at 1.8A resolution. The structures of the native creatininase and the Mn-activated
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