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  • Title: Atrioactivase, a specific peptidase in bovine atria for the processing of pro-atrial natriuretic factor. Purification and characterization.
    Author: Imada T, Takayanagi R, Inagami T.
    Journal: J Biol Chem; 1988 Jul 05; 263(19):9515-9. PubMed ID: 2967825.
    Abstract:
    A seryl protease which catalyzes conversion of proatrial natriuretic factor (ANF) to the active circulating form, ANF(99-126), was purified from a particulate fraction of bovine atria. The enzyme was solubilized with 1.6 M KCl. The molecular mass of the purified enzyme was 580 kDa on gel filtration, whereas by sodium dodecyl sulfate-polyacrylamide gel electrophoresis a cluster of six bands with molecular masses around 30 kDa was observed. The purified enzyme produced ANF(99-126) from partially purified bovine pro-ANF by the selective cleavage of the arginyl peptide bond in the -Pro97-Arg98-Ser99-sequence in pro-ANF. The enzyme was localized mainly in the microsomal fraction rather than the granule fraction. It is likely that the enzyme selectively cleaves the Arg98-Ser99 peptide bond in pro-ANF during the process of secretion.
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