Identification and isolation of the major core protein from the oncornavirus-like particle in human milk.
Subviral cores have been prepared from the oncornavirus-like particle found in human milks with the use of phospholipase C and ether or Sterox SL. The major protein of these cores has a molecular weight of 27,000 daltons, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This protein is found in the core fractions of reverse transcriptase-positive milks and is absent in negative milks. It is distributed in sucrose gradients only in those fractions containing cores and reverse transcriptase activity. The major core protein of the human milk oncornavirus-like particle is electrophoretically identical to the major core protein of the mouse mammary tumor virus.
D000818:Animals; D002850:Chromatography, Gel; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D004986:Ether; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D008324:Mammary Tumor Virus, Mouse / Q000032:analysis; D008722:Methods; D051379:Mice; D008895:Milk, Human / Q000201:enzymology / Q000382:microbiology*; D008970:Molecular Weight; D009858:Oncogenic Viruses / Q000032:analysis*; D010740:Phospholipases; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism; D014764:Viral Proteins / Q000302:isolation & purification*
D003902:Detergents; D014764:Viral Proteins; D004986:Ether; D012194:RNA-Directed DNA Polymerase; D010740:Phospholipases