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DNA polymerase α‐DNA primase from human placenta Immunoaffinity purification and preliminary characterization
Author(s) -
Podust V.N.,
Lavrik O.I.,
Nasheuer H.-P.,
Grosse F.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80181-4
Subject(s) - primase , dna polymerase , microbiology and biotechnology , polymerase , dna , dna clamp , gel electrophoresis , biology , primer (cosmetics) , dna polymerase ii , biochemistry , human placenta , chemistry , placenta , polymerase chain reaction , reverse transcriptase , gene , fetus , genetics , pregnancy , organic chemistry
Highly purified DNA polymerase α‐DNA primase from normal human tissue (human placenta) has been prepared by immunoaffinity purification on immobilized anti‐human DNA polymerase α monoclonal antibody SJK 287‐38. According to data from SDS electrophoresis this preparation consists of subunits of 180, 160, 145, 140 kDa (a cluster of DNA‐polymerizing subunits), 73 kDa (function unknown) and 59, 52 kDa (corresponding to primase). Three active enzyme forms of 270, 460 and 575 kDa have been revealed using native electrophoresis followed by detection of DNA polymerase activity.