Proteinase isoinhibitors from bovine spleen: primary structure of an intermediate in the processing of the precursor
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference16 articles.
1. Heterogeneity of the Basic Pancreatic Inhibitor (Kunitz) in Various Bovine Organs
2. Primary structure and antiproteolytic activity of a Kunitz-type inhibitor from bovine spleen.
3. Primary structure of a protease isoinhibitor from bovine spleen. A possible intermediate in the processing of the primary gene product.
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. Reversible Inhibitors of Serine Proteinases;Peptides;1995
2. Differential in vitro translation of the precursors of bovine pancreatic trypsin inhibitor and its isoinhibitor II is controlled by the 5′-end region of their mRNAs;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1993-09
3. High-performance liquid chromatographic separation of aprotinin-like inhibitors and their determination in very small amounts;Journal of Chromatography B: Biomedical Sciences and Applications;1993-08
4. Bovine pancreatic trypsin inhibitor and homologous polypeptide inhibitors in nephron cells;Peptides;1992-03
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