PubMed Health⌕ Search

Biomedical subjects

E Erikson

Publications and source records attributed to E Erikson.

70 records · Page 4Linked to original sources
PubMed1978

Identification of a polypeptide encoded by the avian sarcoma virus src gene.

Two techniques were used to search for the polypeptide encoded by the avian sarcoma virus (ASV) src gene. First, antiserum from rabbits bearing ASV-induced fibrosarcomas was used to immunoprecipitate a transformation-specific antigen from ASV-transformed chick embryo fibroblasts. This antigen has an apparent molecular weight (Mr) of 60,000. Second, the 3' one-third of the ASV genome, selected by oligo(dT)-cellulose chromatography and sucrose gradient sedimentation, was translated in a mRNA-dependent reticulocyte cell-free lysate. This RNA species programmed the synthesis of a polypeptide that comigrated with the transformation-specific antigen of Mr 60,000 immunoprecipitated from transformed cells. The methionine-containing tryptic peptides from the polypeptides of Mr 60,000 obtained from translation in vitro and from immunoprecipitation were found to be identical upon two-dimensional fractionation.

Alpharetrovirus↗
PubMed1978

Peptide analysis of the transformation-specific antigen from avian sarcoma virus-transformed cells.

Sera from rabbits bearing tumors induced by avian sarcoma virus (ASV) were ussed to immunopecipitate virus-specific proteins from extracts of chicken, hamster, and field vole cells transformed by ASV. Two virus-specific proteins having molecular weights of 76,000 and 60,000 were found in all cell lines examined. The 76,000-molecular-weight protein, Pr76, is the precursor to the internal core proteins of ASV. The 60,000-molecular-weight (60K) transformation-specific antigen from each cell line was subjected to peptide analysis, using chymotrypsin and Staphylococcus aureus V8 protease. The resulting peptide maps of the 60K protein from the different ASV-infected cell types were similar for each enzyme, strongly suggesting that the 60K protein is virus coded. Two-dimensional analysis of chymotryptic peptides from Pr76 and 60K reveals that 60K is not related to the gs antigen precursor. Radiolabeling of ASV-transformed cells with inorganic phosphate revealed that 60K is phosphorylated in vivo. The 60K proteins isolated from both ASV-transformed chicken and field vole cells were found to contain one tryptic phosphopeptide. The tryptic phosphopeptides of 60K from both cell lines migrated identically upon two-dimensional peptide analyses, and their migration differed from that of the principal phosphopeptide of Pr76.

Alpharetrovirus↗
PubMed1977

Translation of 35S and of subgenomic regions of avian sarcoma virus RNA.

Rabbit antiserum monospecific for an internal structural protein, p27, of avian sarcoma viruses (ASV) was found to immunoprecipitate polypeptides with molecular weights (Mr) of 180,000 and 76,000 from cell-free reticulocyte lysates programmed by ASV 35S RNA and also from lysates of ASV-infected cells. In addition, the Mr 180,000 protein was also precipitated by antiserum raised against virion DNA polymerase, suggesting that is a product of the two genes nearest the 5' end of virion 35S RNA. We have also investigated the ability of subgenomic portions of virion RNA to program cell-free protein synthesis. A 10-12S poly(A)-containing fragment of RNA from both nondefective and transformation-defective ASV directed the synthesis of a polypeptide of Mr 29,000 immunologically unrelated to the gs antigens; 20-24S poly(A)-containing RNA from nondefective ASV directed the synthesis of a polypeptide of Mr 60,000 not found when a similar RNA preparation from transformation-defective ASV was translated, suggesting that it is the product of the ASV src gene. These results indicate that internal initiation sites for protein synthesis exist on the 35S RNA genome.

Avian Sarcoma Viruses↗
PubMed1974

The 7S RNA common to oncornaviruses and normal cells is associated with polyribosomes.

The 7S RNA species first demonstrated in avian and murine oncornaviruses and later in normal, uninfected cells is found associated in part with cellular polyribosomes. A molar ratio of 7S RNA to 5S ribosomal RNA of 0.05 indicates that there is approximately one mole of 7S RNA per mole of messenger RNA. Dissociation of polyribosomes with dimethylsulfoxide results in a marked decrease in the sedimentation rate of the 7S RNA. The dimethylsulfoxide-induced dissociation of polyribosomes and the concomitant movement of the 7S RNA from the polyribosome region into lighter regions of a sucrose gradient are both inhibited by cycloheximide, indicating that the 7S RNA is indeed associated with polyribosomes and not with a ribonucleoprotein particle sedimenting with polyribosomes.

Animals↗
PubMed1971

Association of 4S ribonucleic acid with oncornavirus ribonucleic acids.

Oncornavirus 60 to 70S ribonucleic acids (RNA), such as those from avian myeloblastosis virus, Schmidt-Ruppin virus, or mouse sarcoma-mouse leukemia viruses, isolated by conventional techniques, contain 4S transferlike RNA molecules that are released upon dissociation of the 60 to 70S RNA with heat. The 4S RNA represents 2.5 to 3.0% of the RNA in the 65S aggregate or 4 to 5 molecules per molecule of 35S RNA formed.

Autoradiography↗
PubMed1967

Structure and function of bacteriophage R17 replicative intermediate ribonucleic acid. II. Properties of the parental labeled molecule.

Replicative intermediate ribonucleic acid (RNA), designated RI, which contained parental RNA labeled with (32)P was separated by filtration through agarose from the nucleic acids prepared from (32)P-labeled RNA phage-infected Escherichia coli. A larger amount of ribonuclease-sensitive parental label was found in the rapidly sedimenting forms of RI than in the slower sedimenting forms, indicating that parental RNA is displaced to form a single-stranded tail. This result indicates that some phage RNA is generated by asymmetric semiconservative replication of RI, but it does not mean that a portion of the RI duplexes cannot be conserved during generation of phage RNA. Parental RNA was also found in double-stranded RNA with no apparent tails which sedimented with an S value of 13. This RNA was soluble in 2 m NaCl, and its sedimentation rate was unaffected by ribonuclease; nevertheless, single-strand scissions were produced by ribonuclease and were detected after the duplex was converted to its component single strands.

Coliphages↗