A8200
氨基肽酶 来源于溶解蛋白单孢菌
lyophilized powder, 50-150 units/mg protein
别名:
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
等级
Proteomics Grade
质量水平
表单
lyophilized powder
比活
50-150 units/mg protein
分子量
29.5 kDa
组成
Protein, ~40% biuret
溶解性
H2O: soluble 0.9-1.1 mg/mL, clear, colorless
异质活性
endopeptidase, essentially free
储存温度
−20°C
一般描述
一种含锌的酶。
应用
氨肽酶是一类分布广泛的蛋白酶家族，可用于研究蛋白质成熟、激素产生、吸收消化等许多重要的生物学过程。这种酶已被用来测量bestatin（一种蛋白酶抑制剂）与氨肽酶结合的动力学速率常数。
生化/生理作用
蛋白水解气单胞菌的氨肽酶参与蛋白质成熟、激素生成和肽消化。
蛋白质气单胞菌氨肽酶是一种金属酶，通过重组法测得，氨肽酶在一个单体中含有2个zn2 +原子，分子量约为29.5 kDa。这种酶具有高度的稳定性，即使在70℃的温度下也可稳定数小时。部分失活发生在8 M尿素中。最大的稳定性和活性在pH 8.0-8.5之间。蛋白纯化气单胞菌的氨肽酶可发挥酯酶的作用。
催化释放 N -末端氨基酸，优先释放亮氨酸，而不是谷氨酸或天冬氨酸。
外形
含 tricine 缓冲液（pH 8.0）、氯化锌和稳定剂的冻干粉。
制备说明
以0.9-1.1 mg / mL的浓度溶于水，形成澄清的无色溶液。
其他说明
在25℃、pH 8.0条件下，每分钟可将1.0μ956摩尔的L-亮氨酸对硝基苯胺水解为L-亮氨酸和对硝基苯胺。
警示用语：
Danger
危险分类
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
James Kahn et al.
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 38(4), 238-241 (2011-05-14)
We have recently designed a biochemistry laboratory experiment for the purpose of providing students an advanced experience with enzyme kinetics and the kinetics of binding. Bestatin, a well-known and commercially available general protease inhibitor, is a slow-binding inhibitor of aminopeptidase
David L Bienvenue et al.
Biochemistry, 42(36), 10756-10763 (2003-09-10)
The catalytic and structural properties of divalent metal ion cofactor binding sites in the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae were investigated. Co(II)-substituted DapE enzyme was 25% more active than the Zn(II)-loaded form of the enzyme. Interestingly, Mn(II)
Brian Bennett et al.
Journal of the American Chemical Society, 124(44), 13025-13034 (2002-10-31)
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monosubstituted AAP exhibited an axial Cu(II)
S Nirasawa et al.
The Biochemical journal, 341 ( Pt 1), 25-31 (1999-06-23)
An aminopeptidase from Aeromonas caviae T-64 was translated as a preproprotein consisting of three domains; a signal peptide (19 amino acid residues), an N-terminal propeptide (101 residues) and a mature region (273 residues). We demonstrated that a proteinase, which was
William T Desmarais et al.
Structure (London, England : 1993), 10(8), 1063-1072 (2002-08-15)
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution
我们的科学家团队拥有各种研究领域经验，包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持