Bovine pancreatic trypsin inhibitor and homologous polypeptide inhibitors in nephron cells.
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).
Nori
S L
SL
Institute of Anatomy, Catholic University, Rome, Italy.
De Renzis
G
G
Fumagalli
L
L
Fioretti
E
E
Barra
D
D
Ascoli
F
F
D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000032:analysis* / Q000302:isolation & purification; D002417:Cattle; D007150:Immunohistochemistry; D009399:Nephrons / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000737:chemistry* / Q000302:isolation & purification
D010455:Peptides; D011480:Protease Inhibitors; D007611:Aprotinin