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Total purification of a DNA‐dependent ATPase and of a DNA‐binding protein from human cells.
Author(s) -
Biamonti G.,
Cobianchi F.,
Falaschi A.,
Riva S.
Publication year - 1983
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1983.tb01399.x
Subject(s) - biology , microbiology and biotechnology , dna , genetics , humanities , philosophy
We have purified to near homogeneity the major DNA‐dependent ATPase from human cells. The pure enzyme has a mol. wt. of 68,000 and a minimum specific activity of approximately 150 U/mg. When the properties of the pure enzyme are compared with those of a less purified preparation, significant differences are observed both in structure and in function. These can be ascribed to the interaction of the ATPase with a DNA‐binding protein (mol. wt. 28,000) that we can also purify to near homogeneity from the same cells and which is present in the less purified preparations of the ATPase. The ability of the less purified ATPase to stimulate DNA polymerase alpha in helicase fashion is probably due to the presence of the DNA‐binding protein.