Bovine pancreatic trypsin inhibitor and homologous polypeptide inhibitors in nephron cells

Peptides. 1992 Mar-Apr;13(2):365-71. doi: 10.1016/0196-9781(92)90122-j.

Abstract

Bovine pancreatic trypsin inhibitor (BPTI, aprotinin) is a fifty-eight amino acid polypeptide, which is present together with related molecular isoforms in various bovine organs. In the present study these protease inhibitors were isolated from bovine kidney by affinity chromatography on immobilized trypsin and a subsequent FPLC step. Due to their electrophoretic, structural, and inhibitory properties, the inhibitors were strictly similar to the polypeptides identified previously in other bovine organs. Immunohistochemical experiments showed a widespread localization of these polypeptides in nephron epithelial cells (proximal and distal tubules, loop of Henle, collecting tubules).

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aprotinin / analysis*
  • Aprotinin / isolation & purification
  • Cattle
  • Immunohistochemistry
  • Nephrons / chemistry*
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / isolation & purification

Substances

  • Peptides
  • Protease Inhibitors
  • Aprotinin