PEPTIDE-MAPPING OF THE 4 SUBUNITS OF THE MOUSE DNA-POLYMERASE ALPHA-PRIMASE COMPLEX

被引：27

作者：

TAKADATAKAYAMA, R ^{[1
]}

TADA, S ^{[1
]}

HANAOKA, F ^{[1
]}

UI, M ^{[1
]}

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,TOKYO 113,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 170卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92132-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We report a simple, two-step method (phosphocellulose and immunoaffinity column chromatographies) for purification of the mouse DNA polymerase α-primase complex. The advantages of this method over other procedures are its simplicity and rapidity, with little loss by proteolysis. Sedimentation analysis in a glycerol density gradient of the immunoaffinity-purified fraction revealed that four polypeptides with molecular weights of 180,000, 68,000, 54,000 and 46,000 in the enzyme fraction form a physical complex. Peptide mapping by reversed phase-high performance liquid chromatography demonstrated unequivocally that these four polypeptides constituting the complex are different entities. © 1990.

引用

页码：589 / 595

页数：7

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