DNA-Dependent RNA-Directed Protein Synthesis in vitro, IV. Peptide Analysis of an in vitro and in vivo φ X174 Structural Protein

An antibody-precipitable structural protein from the bacteriophage φ X174 was purified from an in vitro protein-synthesizing system primed with the replicative DNA of the virus. This protein was trypsin digested in the presence of the differentially labeled analogous protein that was purified from t...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 67; no. 1; pp. 13 - 17
Main Authors Gelfand, David H., Hayashi, Masaki
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.09.1970
National Acad Sciences
Subjects
Amino acids
Amino Acids - metabolism
Antigen-Antibody Reactions
Bacteriophages
Biochemistry
Biological Sciences: Biochemistry
Carbon Isotopes
Chemical suspensions
Chromatography
Chromatography, Ion Exchange
Coliphages
DNA
DNA, Viral
Electrophoresis
Gels
Peptides - analysis
Radiocarbon
Resins
Tritium
Trypsin
Viral Proteins - biosynthesis
Viral Proteins - isolation & purification
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Summary:An antibody-precipitable structural protein from the bacteriophage φ X174 was purified from an in vitro protein-synthesizing system primed with the replicative DNA of the virus. This protein was trypsin digested in the presence of the differentially labeled analogous protein that was purified from the bacteriophage. The tryptic hydrolysate was subjected to high resolution peptide chromatography which revealed essentially identical patterns for the φ X174 proteins synthesized in vitro and in vivo.
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Requests for reprints may be addressed to Dr. D. H. Gelfand, Department of Biology, University of California, San Diego, Revelle College, La Jolla, Calif. 92037.
This work was supported, in part, by a U.S. Public Health Service research grant (GM-12934) and a National Science Foundation research grant (GB-11873). One of us (D.H.G.) was the recipient of a U.S. Public Health Service predoctoral traineeship grant (GM-00702) and the other (M.H.) is the recipient of a career development research award from the U.S. Public Health Service (GM-42360).
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.67.1.13