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 Corn Trypsin Inhibitor (CTI)

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Haematologic Technologies, Inc.

57 River Road

Essex Junction, VT USA

Tel: 802.878.1777

Fax: 802.878.1776

Email: hti@haemtech.com

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EFFECT OF CTI ON THE APTT AND PT OF NORMAL HUMAN PLASMA.  The graph illustrates the effect of added CTI on the PT and aPTT of normal human plasma.  CTI was added to normal pooled human plasma to various final concentrations, and the mixtures were allowed to incubate for a brief period on ice prior to conducting the assays.  The PT remains unaffected while the aPTT doubles with the addition of approximately 60 micrograms of CTI per ml of plasma.

Corn trypsin inhibitor (CTI) is a small protein that is localized in the kernels of most species of corn. CTI is not only an inhibitor of trypsin, but is also a specific human factor XIIa inhibitor when tested in blood clotting experiments (1-6). The inhibitor forms a one-to-one complex with either trypsin or factor XIIa, and when added to plasma, prolongs the activated partial thromboplastin time without affecting the PT assay (6). The specificity for factor XIIa makes the inhibitor useful for the segregation and study of coagulation reactions (6). 


The protein is comprised of 112 amino acids which yields a calculated molecular weight of 12,028 (7). The calculated molecular weight and that which has been determined by sedimentation equilibrium analyses of the purified protein (12,500) are in good agreement (3). A comparison of the amino acid sequence of CTI to that of other trypsin or serine protease inhibitors reveals little or no similarities (7). 

CTI is purified using a combination of published procedures (3,4). To begin the purification process, CTI is extracted from the kernels of fresh sweet corn into a physiologic buffer. The extract is then de-fatted using acetone, and the protein is further purified by employing gel filtration and ion-exchange chromatography. The final CTI preparation appears as a single band by SDS-PAGE analyses under both reducing and non-reducing conditions. 

Preparations of CTI are tested for the ability to prolong the aPTT assay without affecting the PT assay. The specific activity of each lot of CTI is determined, and one unit is defined as the amount of CTI required to double the aPTT of normal human plasma. 

Purified CTI is formulated in 20 mM Tris, 0.15 M NaCl, pH 7.4 and should be stored frozen at -20°C or colder. 

Blood Collection Tubes

To simplify the process of collecting samples with added CTI, HTI has developed blood collection tubes containing CTI. These tubes simplify the process of conducting TF-dependent studies by allowing you to draw blood directly onto an anticoagulant containing CTI. You may choose to use our standard CTI/Citrate formulation (11mM Citrate, 50 ug/mL CTI) or you may create your own custom formulation. HTI’s blood collection tubes are not sterile and are manufactured and sold for research use only.

 

DOWNLOAD CORN TRYPSIN INHIBITOR APPLICATION PDF

Properties of Corn Trypsin Inhibitor

Localization: Corn Kernals
Mode of action: forms a one-to-one complex with either trypsin or factor XIIa and inhibits their respective catalytic activity.
Molecular weight: 12,500 (3)
Extinction coefficient:
E
1 %
1 c m, 280 nm
= 20.0 (determined by ultra centrifugation studies)
Structure: single chain protein comprised of 112 amino acids (3,7)

 

Catalog Number

Description

CTI-01

Corn Trypsin Inhibitor

SCAT-27-4.5/5

CTI/Citrate Blood Collection Tube

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References 
1. Hochstrasser, K., et al., Z. Physiol. Chem., 348, 1337 (1967). 
2. Halim, R.K., et al., Crop. Sci., 13, 405 (1973). 
3. Swartz, M.J., et al., J. Biol. Chem., 252, 8105 (1977). 
4. Hojima, Y., et al., Thromb. Res., 20, 149 (1980). 
5. Ratnoff, O.D. and Moneme, V., Proc. Soc. Exp. Biol. Med., 166, 297 (1981). 
6. Rand, M.D. et al., Blood, 88, 3432 (1996). 
7. Mahoney, W.C., et al., J. Biol. Chem., 259, 8412 (1984).

 

 Please inquire about products not listed.  We can also custom purify proteins from other species. 

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