Isolation of proteins with kinase activity and related to pp60 src from human cells

A protein kinase activity (PK) was associated with immunoprecipitates between polypeptides of human lymphoblastoid cells of malignant origin (Raji cell line) or of their normal counterparts (Priess cell line) and antibodies directed against avian pp60 src or against the carboxyterminal hexapeptide o...

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Published inBiochemical and biophysical research communications Vol. 121; no. 3; pp. 779 - 787
Main Authors Pavloff, Nadine, Biquard, Jean-Michel, Hanania, Nicole, Semmel, Marianne
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 29.06.1984
Subjects
Animals
Autoradiography
Avian Sarcoma Viruses
Burkitt Lymphoma
Cell Line
Cell Transformation, Viral
Chick Embryo
Epitopes - isolation & purification
genes
Humans
Immunochemistry
Lymphocytes - analysis
man
Neoplasm Proteins - isolation & purification
Oncogene Protein pp60(v-src)
protein kinase
Protein Kinases - isolation & purification
Raji cells
Sarcoma, Experimental
Viral Proteins - isolation & purification
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Summary:A protein kinase activity (PK) was associated with immunoprecipitates between polypeptides of human lymphoblastoid cells of malignant origin (Raji cell line) or of their normal counterparts (Priess cell line) and antibodies directed against avian pp60 src or against the carboxyterminal hexapeptide of pp60 src. Therefore, these human cells and Rous Sarcoma Virus (RSV) transformed avian cells share antigenic determinants of pp60 src and, in particular, its carboxyterminal sequence, as well as one of its functions, a protein kinase activity. The protein kinase from Raji cells phosphorylated predominantly tyrosine residues, that from Priess cells threonine residues.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(84)90746-0