title: In vitro studies on the conversion of the biosynthetic precursor of renin.
abstract: The initial translation product of mouse submaxillary gland mRNA has a molecular weight of about 50,000. We have now translated renin mRNA in frog oocytes which are known to be able to remove the so-called "pre"- or "signal"- sequence from products of injected mRNAs. From these injected oocytes, we could precipitate with antirenin a 48,000 dalton polypeptide. Treatment with kallikrein or trypsin of the oocyte product resulted in a decrease in amount of this 48,000 dalton protein and a corresponding increase in a 45,000 dalton protein, precipitable with antirenin. We conclude that the initial translation product of renin mRNA is a preprorenin of molecular weight 50,000, which in oocytes is enzymatically cleaved to render 48,000 dalton prorenin. Although kallikrein may be a physiological activator of renin, it appears to be not the only one since no mature, 40,000 dalton renin was formed.
mesh_terms: D000818:Animals; D003080:Cold Temperature; D004792:Enzyme Precursors / Q000235:genetics*; D005260:Female; D051379:Mice; D009865:Oocytes / Q000378:metabolism; D011061:Poly A / Q000235:genetics; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics; D012083:Renin / Q000235:genetics*; D013363:Submandibular Gland / Q000201:enzymology*; D014981:Xenopus
chemical_list: D004792:Enzyme Precursors; D012333:RNA, Messenger; D011061:Poly A; D012083:Renin