The restriction endonuclease Pal1 was purified from Providencia alcalifaciens 1650-fold with a yield of 33%. The purified protein moved as a single band upon polyacrylamide gel electrophoresis. When this was carried out in the presence of sodium dodecyl sulfate, a molecular weight of 31,000 was obta
Rapid purification of a restriction endonuclease fromEscherichia coliRY13
β Scribed by R. S. Mehra; V. P. Malhotra; G. W. Rembhotkar
- Book ID
- 104646503
- Publisher
- Springer-Verlag
- Year
- 1993
- Tongue
- English
- Weight
- 338 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0951-208X
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β¦ Synopsis
A two step method for the purification of restriction endonuclease Eco RI was developed. The first step involved the purification of the enzyme on Cibacron Blue-F3GA-agarose column, followed by a hydroxyapatite column. The enzyme was homogeneous on SDS-PAGE and completely free from contaminating nucleases and phosphatases, and can be used for direct DNA hydrolysis.
π SIMILAR VOLUMES
A physical map of the actinophage VWB has been constructed using the restriction endonucleases BglII, ClaI, EcoRI, EcoRV, HindIII, KpnI and SphI. Phage VWB, genome size 47.3 kb, propagates on Streptomyces venezuelae, and it can also lysogenise this species. The three BglII-generated fragments of VWB