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Merck

P2143

Sigma-Aldrich

蛋白酶 来源于佐氏曲霉

Type XIII, ≥0.6 unit/mg solid

别名:

Molsin

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About This Item

CAS号:
EC 号:
MDL编号:
UNSPSC代码:
12352204
eCl@ss:
32160410
NACRES:
NA.54

生物来源

Aspergillus sp. (Aspergillus saitoi)

类型

Type XIII

表单

solid

比活

≥0.6 unit/mg solid

异质活性

alkaline protease, essentially free

储存温度

−20°C

相关类别

应用

Aspergillus saitoi来源蛋白酶已用于一项评估大蛋白氢交换序列覆盖率和分辨率的研究中。它还被用于一项通过β-葡萄糖苷酶研究大豆凝乳异黄酮糖苷向其糖苷配基转化的研究中。

生化/生理作用

Aspergillus saitoi来源蛋白酶也可发挥β-葡萄糖苷酶的作用。

单位定义

在pH 2.8、37℃条件下,一单位每分钟可水解酪蛋白并产生相当于1.0 μ摩尔 (181 μg) 酪氨酸的显色(使用Folin-Ciocalteu试剂显色)。

象形图

Health hazardExclamation mark

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 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

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R E Cardoza et al.
Biotechnology and bioengineering, 83(3), 249-259 (2003-06-05)
A copy of the bovine chymosin gene (chy) with a codon usage optimized for its expression in Aspergillus awamori was constructed starting from synthetic oligonucleotides. To study the ability of this filamentous fungus to secrete bovine prochymosin, two plasmids were
M E Kambouris et al.
FEMS immunology and medical microbiology, 25(3), 255-264 (1999-08-25)
In immunodeficient patients, Aspergillus species emerge as circumstantial pathogens. Aspergillus fumigatus is a distant first among the pathogenic aspergilli, which cause deep-seated mycoses. Sequences of the pep gene of A. fumigatus as potential PCR primers, which have not been tested
E Skyttä et al.
The Journal of applied bacteriology, 74(2), 134-142 (1993-02-01)
The broad-spectrum antibacterial activity exhibited by three Pediococcus strains isolated from beer was preliminarily characterized. Factors affecting the production rate of bacterial inhibitors were screened and the effects of simultaneous cultivation of Lactococcus and Pediococcus on the production of inhibitory
I E Mattern et al.
Molecular & general genetics : MGG, 234(2), 332-336 (1992-08-01)
In the present study, the extracellular protease activity in a strain of the filamentous fungus Aspergillus niger was investigated and mutant strains deficient in the production of extracellular proteases were isolated. The major protease, which is responsible for 80-85% of
S W Cho et al.
Acta crystallographica. Section D, Biological crystallography, 57(Pt 7), 948-956 (2001-06-22)
The crystal structure of aspergillopepsin I (AP) from Aspergillus phoenicis has been determined at 2.18 A resolution and refined to R and R(free) factors of 21.5 and 26.0%, respectively. AP has the typical two beta-barrel domain structure of aspartic proteinases.

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