Structure of DNA polymerase alpha-primase complexes from mammalian cells analyzed by using monoclonal antibodies.
The molecular masses of two of the four DNA polymerase alpha-primase complex subunit peptides from various mammalian cells have been compared through the use of specific monoclonal antibodies. One monoclonal antibody (E4) binds to 77-kDa peptide from HeLa cells and cognate peptides from other mammalian cells (monkey, mouse, bovine, Indian muntjac, and hamster). Another monoclonal antibody (A5) binds the 180-kDa type peptide and its degradation product (160-kDa peptide) of the mammalian DNA polymerase alpha-primase complexes. Neither of these antibodies reacts with DNA polymerase alpha-primase complex from chicken cells. Comparative immunoblot analysis indicates that the molecular masses of the two main peptides of DNA polymerase alpha-primase complex isolated from the various mammalian sources are in excellent agreement with each other, except for the 77-kDa type peptide from bovine and Indian muntjac cells which was found to be significantly smaller (68 kDa) in these cases. The small molecular mass of bovine 77-kDa type peptide is not attributable to the action of a protease which may be present in the extract of bovine cells.
Kozu
T
T
Department of Immunology and Virology, Saitama Cancer Center Research Institute.
Nikaido
K
K
Yagura
T
T
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D015153:Blotting, Western; D002417:Cattle; D002478:Cells, Cultured; D006224:Cricetinae; D003429:Cross Reactions; D004257:DNA Polymerase II / Q000276:immunology / Q000302:isolation & purification*; D019915:DNA Primase; D000882:Haplorhini; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D008970:Molecular Weight; D011487:Protein Conformation; D012316:RNA Nucleotidyltransferases / Q000276:immunology / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases; D004257:DNA Polymerase II