The Reactive Sites of Kunitz Bovine-Trypsin Inhibitor. Role of Lysine-15 in the Interaction with Chymotrypsin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1975.tb04110.x/fullpdf
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2. Strukturuntersuchungen am Kallikrein-Inaktivator aus Rinderlunge
3. Notizen: Zur Identität des Kallikrein-Inaktivators aus Rinderlunge und Rinderparotis
4. IDENTITY OF TRYPSIN INHIBITORS ISOLATED FROM BOVINE LIVER and PANCREAS
5. Isolation of a trypsin inhibitor (Kunitz inhibitor) from bovine ovary by affinity chromatography through trypsin-sepharose
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1. Purification and Partial Characterization of Trypsin-Specific Proteinase Inhibitors from Pigeonpea Wild Relative Cajanus platycarpus L. (Fabaceae) Active against Gut Proteases of Lepidopteran Pest Helicoverpa armigera;Frontiers in Physiology;2016-09-07
2. Functional Kunitz inhibitor binding domain in plasmin-derived light chain as shown by affinity chromatography;International Journal of Peptide and Protein Research;2009-01-12
3. ARGININE MODIFICATION IN KUNITZ BOVINE TRYPSIN INHIBITOR THROUGH 1, 2-CYCLOHEXANEDIONE*;International Journal of Peptide and Protein Research;2009-01-12
4. The kinetics of plasmin inhibition by aprotinin in vivo;Thrombosis Research;2005-01
5. Bovine pancreatic elastase II cleaves Gln-Ile bond;Journal of Protein Chemistry;2001
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