@article{mbs:/content/journal/jgv/10.1099/0022-1317-66-5-945, author = "Gallick, G. E. and Sparrow, J. T. and Singh, B. and Maxwell, S. A. and Stanker, L. H. and Arlinghaus, R. B.", title = "Recognition of mos-related Proteins with an Antiserum to a Peptide of the v-mos Gene Product", journal= "Journal of General Virology", year = "1985", volume = "66", number = "5", pages = "945-955", doi = "https://doi.org/10.1099/0022-1317-66-5-945", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-66-5-945", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "Mo-MuSV", keywords = "protein recognition", keywords = "v-mos gene", keywords = "peptide antibody", abstract = "SUMMARY A mos-specific antiserum was generated by injection of rabbits with a peptide predicted from the sequence of the v-mos gene of Moloney murine sarcoma virus (MuSV) strain 124. The peptide is composed of amino acids 37–55 (cyclized at the cysteine residues) conjugated to keyhole limpet haemocyanin. This serum [anti-mos(37–55c)] specifically recognized p37mos in MuSV-124 acutely infected NIH-3T3 cells, P85gag-mos in 6m2 cells, an NRK clone infected with the temperature-sensitive mutant (ts110) of Moloney MuSV, and P100gag-mos in 54-5A4 cells, an NRK clone infected with a spontaneous revertant of ts110. An additional protein of M r 55000 from uninfected cells was recognized by this serum. Reactivity of the serum toward the v-mos-containing proteins and the 55K protein was completely inhibited by prior incubation with free peptide. The 55K protein was not recognized by antisera made from synthetic peptides prepared from the C-terminal eight or 12 amino acids of v-mos.", }