Purification and partial characterization of a Schizolobium parahyba chymotrypsin inhibitor.

Schizolobium parahyba seed chymotrypsin inhibitor (SPC) is a protein with M(r) of 20,000 and four half-cystine residues and no free thiol group. SPC is stable at temperatures up to 75 degrees at pH 7 but gradually loses activity when kept at 95 degrees for 1 hr and total inactivation occurs after 5 hr. Amino acid analysis shows a high content of glycine, aspartate, glutamate and alanine residues. A pI of 4.52 predicted from the amino acid content agrees with experimental results. A stable binary complex with M(r) of 45,000, Ki = 5.85 x 10(-8) M and molar ratio of 1:1 is formed between SPC and chymotrypsin. The determined single N-terminal sequence of SPC shows homology with Kunitz type soybean trypsin inhibitors.