Analysis of the Complex Formed by Erythrina variegata Chymotrypsin Inhibitor with Chymotrypsin and Properties of the Peptides Prepared from the Inhibitor by a Limited Proteolysis
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1997.t01-1-00870.x/fullpdf
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1. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution
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1. Erythrina variegata;Edible Medicinal And Non-Medicinal Plants;2013-09-03
2. Contribution of Conserved Asn Residues to the Inhibitory Activities of Kunitz-Type Protease Inhibitors from Plants;Bioscience, Biotechnology, and Biochemistry;2005-01
3. Protein and Non-Protein Protease Inhibitors from Plants;Bioactive Natural Products (Part J);2003
4. Chymotrypsin Inhibitor from Erythrina variegata Seeds: Involvement of Amino Acid Residues within the Primary Binding Loop in Potent Inhibitory Activity toward Chymotrypsin;Journal of Biochemistry;1998-09-01
5. Cloning and Nucleotide Sequence of the Gene Encoding a Serine Proteinase Inhibitor Named Marinostatin from a Marine Bacterium,Alteromonassp. Strain B-10-31;Bioscience, Biotechnology, and Biochemistry;1998-01
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