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Common Precursor for Rauscher Leukemia Virus gp69/71, p15(E), and p12(E)
- Source :
- Journal of Virology. 23:787-798
- Publication Year :
- 1977
- Publisher :
- American Society for Microbiology, 1977.
-
Abstract
- Rauscher murine leukemia virus glycoprotein gp69/71 and non-glycosylated p15(E) are synthesized by way of a 90,000-dalton precursor glycoprotein, termed Pr2 a + b . Peptide mapping experiments showed that Pr2 a + b contains all the tyrosine-containing tryptic peptides of gp69/71. Two additional tyrosine-containing tryptic peptides in Pr2 a + b that are not detected in gp69/71 are found in p15(E). Thus, gp69/71 and p15(E) peptide sequences account for all the tyrosine tryptic peptides of Pr2 a + b . The gene order of the two proteins was determined by pulse-labeling infected cells in the presence and absence of pactamycin at concentrations of the inhibitor that prevent initiation of translation, but not elongation. The gene order was found to be: 2 HN-gp69/71-p15(E)-COOH. A newly identified major viral protein, termed p12(E), migrates in sodium dodecyl sulfate-polyacrylamide gels in the “p12” region. It is related to p15(E) as determined by tryptic mapping experiments. p15(E) and p12(E) are not phosphorylated, and both can be separated from phosphoprotein p12 by guanidine hydrochloride-agarose chromatography. p12(E) and p15(E) elute in the void volume fraction, whereas phosphoprotein p12 elutes between p15 and p10. The two p12 proteins can also be separated from each other by two-dimensional gel electrophoresis involving isoelectric focusing in the first dimension and sodium dodecyl sulfate-gel electrophoresis in the second dimension.
- Subjects :
- Peptide Biosynthesis
Viral protein
viruses
Immunology
Peptide
Biology
medicine.disease_cause
Rauscher Virus
Microbiology
Viral Proteins
chemistry.chemical_compound
Virology
Animal Viruses
medicine
Protein Precursors
Guanidine
Glycoproteins
Gel electrophoresis
chemistry.chemical_classification
Pactamycin
Isoelectric focusing
Phosphoproteins
Molecular biology
Molecular Weight
Genes
chemistry
Biochemistry
Insect Science
Phosphoprotein
Glycoprotein
Subjects
Details
- ISSN :
- 10985514 and 0022538X
- Volume :
- 23
- Database :
- OpenAIRE
- Journal :
- Journal of Virology
- Accession number :
- edsair.doi.dedup.....8bf8ff9c12abc757ecccd27241471e41
- Full Text :
- https://doi.org/10.1128/jvi.23.3.787-798.1977