Purification of a specific peptidase in bovine atria for the processing of pro-atrial natriuretic factor.
A serine protease which catalyses the conversion of the precursor of ANF (atrial natriuretic factor) to the active circulating form, ANF-(99-126)-octacosapeptide, was purified from a particulate fraction of bovine atria. The enzyme was solubilized with a buffer containing 1.6M KCl. The molecular mass of the purified enzyme was 580 kDa on gel filtration, whereas on sodium dodecyl sulfate-polyacrylamide gel electrophoresis a cluster of six bands with molecular masses around 30 kDa was observed. The purified enzyme produced the ANF-(99-126)-octacosapeptide from partially purified bovine pro-ANF by the selective cleavage of the arginyl peptide bond in the -Pro97-Arg98-Ser99-sequence in pro-ANF. It is likely that the enzyme selectively cleaves the Arg98-Ser99 peptide bond in pro-ANF when ANF is secreted into the circulation.
Imada
T
T
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee.
Takayanagi
R
R
Inagami
T
T
D000818:Animals; D009320:Atrial Natriuretic Factor / Q000378:metabolism*; D002417:Cattle; D002845:Chromatography; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011498:Protein Precursors / Q000378:metabolism*; D011863:Radioimmunoassay; D013050:Spectrometry, Fluorescence
D011498:Protein Precursors; D009320:Atrial Natriuretic Factor; D006493:Heparin; D010447:Peptide Hydrolases