| Literature DB >> 15081278 |
Rozeni C L Teles1, Elizabeth M T de Souza, Leonardo de A Calderon, Sonia M de Freitas.
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.Entities:
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Year: 2004 PMID: 15081278 DOI: 10.1016/j.phytochem.2004.02.002
Source DB: PubMed Journal: Phytochemistry ISSN: 0031-9422 Impact factor: 4.072