A monoclonal antibody which identifies the autophosphorylation domain of autophosphorylating protein kinase 500.
Autophosphorylating protein kinase 500 is a serine protein kinase expressed progressively with the steps of cellular transformation, approaching levels from 50- to 100-fold in the terminal stages of malignancy. The enzyme possesses a sharply restricted range of substrates: itself and a ribosomal protein with a molecular weight of 31,000 (S6). We report here on the characterization of a monoclonal antibody directed against the autophosphorylation domain of AUT-PK 500. The specificity of the antibody is evidenced by blockage of the enzyme phosphorylation without interfering with the native S6 or synthetic octapeptide (S6-1) serine residue phosphorylations. This represents an important step in identifying a probe that can be used to explore the structure and potential function of AUT-PK 500 in cellular transformation.
Majumdar
G
G
Section of Regulatory Biology, Cleveland Clinic Research Institute, Ohio 44195-5068.
Jefferson
W E
WE
Sharma
R K
RK
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D011494:Protein Kinases