- ￥1500
- 阿拉丁
- P128655-1mg
- Endoproteinase Glu-C from Staphylococcus aureus V8
- 2025年10月13日
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- 保存条件：
≥500 units/mg dry weight
- 库存：
Endoproteinase Glu-C from Staphylococcus aureus V8
- 英文名：
Endoproteinase Glu-C from Staphylococcus aureus V8
- 供应商：
66676-43-5
- 规格：
1mg
Endoproteinase Glu-C from Staphylococcus aureus V8
≥500 units/mg dry weight
| 产品名称 | 蛋白内切酶 Glu-C 来源于金黄球菌 V8 |
|---|---|
| 英文名称 | Endoproteinase Glu-C from Staphylococcus aureus V8 |
| 别名 | V8蛋白酶 |
| 英文别名 | V8 Protease;Protease,Staph aureus from Staphylococcus aureus V8 |
| 规格或纯度 | ≥500 units/mg dry weight |
| 运输条件 | 冰袋运输 |
| 单位定义 | One Unit causes a change of 0.001 A280 nm per minute at 37°C, pH 7.8 using casein as the substrate. |
| 酶学委员会编号 | I.U.B.: 3.4.21.19 |
| 生化机理 | Staphylococcus strain V8 protease specifically cleaves peptide bonds on the carboxyl side of aspartic and glutamic acid residues when used in phosphate buffer. When used in ammonium bicarbonate buffer or ammonium acetate buffer cleavage is restricted to the carboxyl side of glutamic acid residues only. The enzyme exhibits maximal activity from pH 4.0 to 7.8. If hemoglobin is used as the substrate, maximal activity is at pH 4.0. The maximal activity is at pH of 7.8 when casein is the substrate. |
一般描述
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).Endoproteinase Glu-C from Staphylococcus aureus strain V8 is a serine protease used for selective cleavage of proteins for amino acid sequence determination or peptide mapping .
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).
Endoproteinase Glu-C from Staphylococcus aureus strain V8 is a serine protease used for selective cleavage of proteins for amino acid sequence determination or peptide mapping .
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