The two-step interaction between α-dimethylaminonaphthalene-1-sulfonyl-pepsinogen-(1–12) and pepsin
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. Interaction of .alpha.-dansylated peptide inhibitors with porcine pepsin: detection of complex formation by fluorescence energy transfer and chromatography and evidence for a two-step binding scheme
2. Peptides: Structure and Biological Function, Proc. Sixth American Peptide Symposium;Dunn,1979
3. Intramolecular Activation of Porcine Pepsinogen
4. Kinetics and Mechanism of Pepsinogen Activation
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Aspartic proteinases and their inhibitors;Biochemical Society Transactions;1985-12-01
2. Cryoenzymology of penicillopepsin. Appendix: Mechanism of Action of Aspartyl Proteinases;Biochemistry;1984-10
3. A new substrate for porcine pepsin possessing cryptic fluorescence properties;Analytical Biochemistry;1983-03
4. Inhibition of pepsin by analogues of pepsinogen-(1–12)-peptide with substitutions in the 4–7 sequence region;Biochemical Journal;1983-02-01
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