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T4385

Sigma-Aldrich

Trypsin inhibitor from turkey egg white

Type II-T

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About This Item

CAS Number:
9035-81-8
EC Number:
232-906-9
MDL number:
MFCD00082102
UNSPSC Code:
12352202

biological source

turkey egg white

type

Type II-T

form

powder

mol wt

~20,000 Da

technique(s)

inhibition assay: suitable

solubility

0.067 M sodium phosphate buffer, pH 7.6: 1 mg/mL, clear, colorless

shipped in

ambient

Storage temp.

2-8°C

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General description

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.

Unit Definition

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.

Analysis Note

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.

Other Notes

View more information on Trypsin Inhibitor.

Pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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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)
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
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
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

Chromatograms

application for HPLC

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