Retention of actin synthesis in liver under conditions that inhibit synthesis of almost all other proteins.
As briefly reported [(1986) Fed. Proc. 45, 1771, Abstr. 1690], rats fed a protein-free diet for a few days often show a marked inhibition of protein synthesis in liver cytosol. However the synthesis of a protein of molecular mass approximately 42 kDa is fully retained. We show here on the basis of its molecular mass, number of bands on isoelectric focusing, isoelectric point and immunological reactivity that this protein is actin and also that actin mRNA is not degraded by micrococcal nuclease under conditions which degrade the bulk of other mRNAs.
D000199:Actins / Q000096:biosynthesis* / Q000235:genetics; D000818:Animals; D001921:Brain / Q000187:drug effects / Q000378:metabolism; D002474:Cell-Free System; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D008836:Micrococcal Nuclease / Q000494:pharmacology; D008970:Molecular Weight; D014176:Protein Biosynthesis / Q000187:drug effects; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D011919:Rats, Inbred Strains
D000199:Actins; D012333:RNA, Messenger; D008836:Micrococcal Nuclease