DNA polymerase α‐DNA primase from human placenta Immunoaffinity purification and preliminary characterization

FEBS Letters

Lavrik, O.I.¹  Podust, V.N.¹  Nasheuer, H.-P.²  Grosse, F.² 

[1] Institute of Bioorganic Chemistry, Siberian Division of the Academy of Sciences of the USSR, Novosibirsk 630090, USSR;Department of Chemistry, Max Planck Institute of Experimental Medicine, D-3400 Göttingen, FRG

关键词: DNA polymerase α;    Immunoaffinity purification;    (Human placenta);   

DOI  :  10.1016/0014-5793(89)80181-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown