In vivo and in vitro phosphoarylation of nuclear proteins in rat liver.
The incorporation of 32P into nuclear nonhistone proteins was compared in rat liver in vivo, in liver slices incubated in vitro, and in isolated nuclei incubated with gamma-[32P]ATP. The highest specific activities of nuclear phosphorproteins were obtained by incubating isolated nuclei. However, the Radioactivity profiles of polyacrylamide gel electrophoretograms of these proteins differed from those obtained in vivo or in liver slice experiments. A group of low molecular weight nonhistone proteins exhibited a very high incporation of labelled phosphate. These proteins could be obtained from the interface when the phosphoproteins were isolated by the buffered phenol extraction procedure. Phosphorylated proteins were also obtained from three cytoplasmic fractions (mitochondria, microsomes, and cytosol). The specific activities of these proteins were much lower than of the nuclear phosphoproteins.
D000818:Animals; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000378:metabolism*; D008297:Male; D009698:Nucleoproteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000096:biosynthesis*; D051381:Rats; D013347:Subcellular Fractions / Q000378:metabolism
D009698:Nucleoproteins; D010750:Phosphoproteins