Extensive purification of DNA polymerase alpha-primase resulted in a marked loss of the DNA polymerase alpha activity. This loss is due partly to the elimination of some basic proteins from the enzyme preparation since the activity of purified enzyme was stimulated 10- to 15-fold by the addition of
Stimulation of DNA polymerase α by a nuclear DNA/protein complex
✍ Scribed by Balabanova, Henny ;Fridlender, Berthold R. ;Anderer, F. Alfred
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 828 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0275-3723
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✦ Synopsis
Abstract
A nuclear DNA complex containing DNA polymerase and SV40 T‐antigen was isolated from nuclei of SV40‐transformed mouse fibroblasts. DNA polymerase could be separated from the complex. The remaining DNA/T‐antigen‐containing complex stimulated DNA polymerase a activity about 10‐fold. The complex contained 4 major proteins with molecular weights of 46, 54, 76, and 94 kilodalton (KD). The stimulation activity was retained by protein A–Sepharose loaded with specific IgG from SV40‐tumor bearer serum, or from antisera against the 94 KD and 76 KD components and was partially inhibited in the presence of these antisera. The stimulation activity was completely abolished by treatment of the complex with trypsin or DNase I.
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