A new polypeptide substrate, Suc-Tyr-Leu-Val-pNA, specific for spleen fibrinolytic proteinase (SFP)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
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1. Synthesis of peptide inhibitors of human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase-like proteinase (ELP);International Journal of Peptide and Protein Research;2009-01-12
2. SYNTHESIS OF SUBSTRATES SPECIFIC FOR HUMAN SPLEEN FIBRINOLYTIC PROTEINASE (SFP);International Journal of Peptide and Protein Research;2009-01-12
3. Characterization of Mutant Neutrophil Elastase in Severe Congenital Neutropenia;Journal of Biological Chemistry;2001-04
4. Liquid chromatographic/atmospheric pressure chemical ionization mass spectrometric analysis of synthetic elastase inhibitor peptide;Biological Mass Spectrometry;1992-10
5. Amino acids and peptides. Part 31. Total synthesis of eglin c. Part 1. Synthesis of a triacontapeptide corresponding to the C-terminal sequence 41–70 of eglin c and related peptides and studies on the relationship between the structure and inhibitory activity against human leukocyte elastase, csthepsin G and α-chymotrypsin;J. Chem. Soc., Perkin Trans. 1;1991
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