期刊论文详细信息
FEBS Letters
Identification of c‐myb (chicken), c‐myb (mouse) and v‐myb (AMV) protein products by immunoprecipitation with antibodies directed against a synthetic peptide
Krchňák, Viktor1  Maly, Antonín2 
[1] Léčiva-Pharmaceuticals, 143 10 Praha, Czechoslovakia;Institute of Molecular Genetics, Czechslovak Academy of Sciences, 166 37 Praha, Czechoslovakia
关键词: Anti-peptide antibody;    Immunoprecipitation;    c-myb protein;    p48c-myb;    (Chicken;    Mouse);    KLH;    keyhole limpet haemocyanin;    AEV;    avian erythroblastosis virus;    AMV;    avian myeloblastosis virus;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    c-onc;    cellular oncogene;    v-myb;    transforming sequence of avian myeloblastosis virus;    Pr76gag;    precursor of gag proteins;    cDNA complementary DNA;    BDB;    bis-diazotized benzidine;    p48;    protein of 48 kDa;    v-onc;    viral transforming sequence;    c-myb;    cellular homologue of the transforming sequence of avian myeloblastosis virus;   
DOI  :  10.1016/0014-5793(86)80874-2
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

A synthetic nonadecapeptide (IL 19) derived from a sequence of v-myb was covalently bound to haemocyanin and used for immunization. Anti-IL 19 serum immunoprecipitated a 75 kDa protein in the lysate of metabolically labelled chicken and murine thymus cells. Presaturation of the serum with IL 19 abolished this immunoprecipitation, thus indicating that the product of c-myb in both chicken and murine thymuses is the 75 kDa protein (p75c-myb). Anti IL 19 serum also precipitated p48c-myb) in the lysate of nonproducer myeloblasts.

【 授权许可】

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