PURIFICATION and PARTIAL CHARACTERIZATION of A SCHIZOLOBIUM-PARAHYBA CHYMOTRYPSIN INHIBITOR
Data
1995-06-01
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Artigo
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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.
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Citação
Phytochemistry. Oxford: Pergamon-Elsevier B.V., v. 39, n. 3, p. 521-525, 1995.