Inhibitor of enteropeptidase and trypsin from bovine duodenum

Mikhailova A.G., Evtyukova N. G., Chupova L.A., Rumsh L.D.
PubMed Id: 9845920
Year: 1998  Volume: 44  Issue: 4  Pages: 338-346
Enteropeptidase inhibitor (DI) was isolated from bovine duodenum during purification ofthis enzyme. DI was purified by affinity chromatography on immobilised trypsin. DIpreparations contain two main components: DI-9 (9 kD) and DI-20 (20 kD). The N-terminalamino acid sequence 1-19 of DI-9 is highly homologous to the Kunitz inhibitor (BPI).Molecular weights of DI-9 and BPI are the same (gel electrophoresis data). Fragment 1-19of DI-9 differs from the corresponding region of BPI only at the position 17: DI-9contains Ala-17 instead of Arg in BPI. The homology of N-terminal amino acid sequence 1-25of DI-20 with the corresponding regions of some phospholipases A2 suggests thatthis protein is a new intestinal phospholipase A2. Inhibitor DI-9 andphospholipase DI-20 are probably isolated in a common lipoprotein complex. The onlyearlier known in vitro inhibitor of enteropeptidase, BPI, was localised in vivo indifferent tissues with this enzyme. in our opinion the Kunitz-type inhibitor DI-9 is, , aphysiological inhibitor of enteropeptidase.
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Keywords: enteropeptidase inhibitor, bovine duodenum, purification, N-terminal amino acid sequence

Mikhailova, A. G., Evtyukova, N. , G., Chupova, L. A., Rumsh, L. D. (1998). Inhibitor of enteropeptidase and trypsin from bovine duodenum. Voprosy Meditsinskoi Khimii, 44(4), 338-346.
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