The Effect of Cleaving the Reactive-Site Peptide Bond Lys-15-Ala-16 on the Conformation of Bovine Trypsin-Kallikrein Inhibitor (Kunitz) as Revealed by Solvent-Perturbation Spectra, Circular Dichroism and Fluorescence
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1975.tb04021.x/fullpdf
Reference16 articles.
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2. 2. M. Laskowski, R. W. Sealock, and P. D. Boyer (1971 ) Enzymes () 3rd edn , 3 , pp.375 -473 , Academic Press, New York.
3. 3. H. Tschesche, R. Obermeier, H. Fritz, and H. Tschesche (1971 ) inProceedings of the Internationsl Research Conference on Proteinase Inhibitors () pp.135 -140 , Walter de Gruyter, Berlin.
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5. Darstellung des aktiven Derivates von Rinder-Trypsin-Kallikrein-Inhibitor (Kunitz) mit im reaktiven Zentrum geöffneter Peptidbindung
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1. Regeneration of native structure and biological activity by air oxidation of the reduced bovine trypsin inhibitor (Kunitz)*;International Journal of Peptide and Protein Research;2009-01-12
2. The Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor): A Milestone Protein;Current Protein & Peptide Science;2003-06-01
3. Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability;Protein Science;2001-04-01
4. ThepH dependence of the equilibrium constantK Hyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin);Journal of Protein Chemistry;1988-10
5. Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor;Journal of Molecular Biology;1983-02
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