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  • Title: Purification and pH stability characterization of a chymotrypsin inhibitor from Schizolobium parahyba seeds.
    Author: Teles RC, de Souza EM, Calderon Lde A, de Freitas SM.
    Journal: Phytochemistry; 2004 Apr; 65(7):793-9. PubMed ID: 15081278.
    Abstract:
    Schizolobium parahyba chymotrypsin inhibitor (SPCI) was completely purified as a single polypeptide chain with two disulfide bonds, by TCA precipitation and ion exchange chromatography. This purification method is faster and more efficient than that previously reported: SPCI is stable from pH 2 to 12 at 25 degrees C, and is highly specific for chymotrypsin at pH 7-12. It weakly inhibits elastase and has no significant inhibitory effect against trypsin and alpha-amylase. SPCI is a thermostable protein and resists thermolysin digestion up to 70 degrees C.
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