DNA polymerase alpha--primase complex of Physarum polycephalum.
DNA polymerase alpha and DNA polymerase alpha--primase complex of Physarum polycephalum were purified by rapid methods, and antibodies were raised against the complex. In crude extracts, immune-reactive polypeptides of 220 kDa, 180 kDa, 150 kDa, 140 kDa, 110 kDa, 86 kDa, 57 kDa and 52 kDa were identified. The structural relationships between the 220 kDa, 110 kDa and 140 kDa (the most abundant form) was investigated by peptide mapping. The 140 kDa form was active DNA polymerase alpha. The 57 kDa and the 52 kDa polypeptides were identified as primase subunits by auto-catalytic labelling. In amoebae, the immune-reactive 140 kDa polypeptide was replaced by a 135 kDa active DNA polymerase alpha.
Achhammer
G
G
Institut für Biophysik and physikalische Biochemie, Regensburg, Germany.
Angerer
B
B
Windisch
C
C
Uhl
A
A
Holler
E
E
D000818:Animals; D019915:DNA Primase; D007120:Immunochemistry; D008970:Molecular Weight; D010449:Peptide Mapping; D016839:Physarum polycephalum / Q000201:enzymology*; D011487:Protein Conformation; D012316:RNA Nucleotidyltransferases / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*
D019915:DNA Primase; D012316:RNA Nucleotidyltransferases