CN
生物来源
turkey egg white
类型
Type II-T
形式
powder
分子量
~20,000 Da
technique(s)
inhibition assay: suitable
溶解性
0.067 M sodium phosphate buffer, pH 7.6: 1 mg/mL, clear, colorless
运输
ambient
储存温度
2-8°C
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一般描述
Ovomucoid or trypsin inhibitor is an abundant protein in most avian egg whites. Three tandem domains are each homologous with pancreatic trypsin inhibitor. It is highly immunogenic, and probably accounts for most cases of egg allergy.
单位定义
One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path.
分析说明
One mg will inhibit 0.9-1.3 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein or 0.4-1.0 mg of α-chymotrypsin with activity of approx. 40 BTEE units per mg protein.
其他说明
查看更多关于 胰蛋白酶抑制剂的信息。
法规信息
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示例
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MMYOMAG-74K-13
1000309185
输入内容 1.000309185)
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Soumika Biswas et al.
Journal of immunology (Baltimore, Md. : 1950), 183(8), 5050-5058 (2009-10-06)
Increased expression of gangliosides by different tumor types including renal cell carcinoma (RCC) is thought to contribute to the immune suppression observed in cancer patients. In this study, we report an increase in apoptotic T cells from RCC patients compared
Identification of the trypsin inhibitor of egg white with ovomucoid.
H LINEWEAVER et al.
The Journal of biological chemistry, 171(2), 565-581 (1947-12-01)
C L Dumke et al.
Journal of applied physiology (Bethesda, Md. : 1985), 92(2), 657-664 (2002-01-18)
Serum proteins [molecular weight (MW) > 10,000] are essential for increased insulin-stimulated glucose transport after in vitro muscle contractions. We investigated the role of the kallikrein-kininogen system, including bradykinin, which is derived from kallikrein (MW > 10,000)-catalyzed degradation of serum
Maurizio Trovato et al.
Biochemical and biophysical research communications, 302(2), 311-315 (2003-02-27)
The design of minimal units required for enzyme inhibition is a major field of interest in structural biology and biotechnology. The successful design of the cyclic dodecapeptide corresponding to the Phe17-Val28 reactive site amino acid sequence of the low-molecular-mass trypsin
I B Svendsen et al.
Carlsberg research communications, 54(6), 231-239 (1989-01-01)
A trypsin inhibitor with a Km of 5 x 10(-5) M has been isolated from kohlrabi (Brassica napus var. rapifera). Subtilisin DY is inhibited only weakly and chymotrypsin not at all. The inhibitor is closely related to napin as determined
Chromatograms
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