Abstract：
: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.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Souza EM,Mizuta K,Sampaio MU,Sampaio CAdoi
10.1016/0031-9422(94)00921-fsubject
Has Abstractpub_date
1995-06-01 00:00:00pages
521-5issue
3eissn
0031-9422issn
1873-3700pii
003194229400921Fjournal_volume
39pub_type
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