Trypsin Inhibitor from Glycine max (soybean) also known as Kunitz trypsin inhibitor is a 21 kDa protein with a single trypsin binding reactive site.
Trypsin Inhibitor from Glycine max (soybean) has been used:
- as a standard protein to measure the amount of endogenous trypsin inhibitor present in midgut lysate (M1) of Riptortus pedestris
- as a standard to compare the trypsin inhibitory activity of the purified protein
- to monitor the trypsin inhibitory activity by fractionating in MonoS cation exchange chromatography
- as an trypsin inhibitor
5, 10, 25 mg in glass bottle
Soybean trypsin inhibitor inhibits trypsin and to a lesser extent chymotrypsin and plasmin. It forms a 1:1 stoichiometric complex with trypsin. Upon formation of this complex, trypsin may cleave a single arginine-isoleucine bond in the inhibitor. Dissociation of this complex may yield the modified form or the native inhibitor. At the optimal pH for trypsin binding (pH 8.0), the association constant is ≥ 10x108.
Trypsin Inhibitor from Glycine max (soybean) binds with the active site of trypsin enzyme, in a competitive inhibition manner.
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.
Further purification of T9128 yielding an electrophoretically pure Kunitz inhibitor with increased activity.
Trypsin inhibitor is soluble in water and phosphate buffers at concentrations of 10 mg/ml or higher. Solutions at higher concentrations may be hazy and have a yellow to amber color.
One mg will inhibit ≥1.0 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.