Top Reasons to buy Deae Cellulose Column Preparation

Top Reasons to Buy Deae Cellulose Column Preparation Deae Cellulose Column Preparation (ion-exchange chromatography) of BSP (Bamboo shoot polysaccharide)! BSP1 eluted with water; BSP2 eluted with 0.05 M NaCl; BSP3 eluted with 0.1 M NaCl; BSP4 eluted with 0.2 M NaCl; BSP5 eluted with 0.5 M NaCl.

The early excision products from irradiated E. coli DNA, isolated by DEAE chromatography, include oligonucleotides of nucleotides in length between 7 and 8. The isolation of these fragments by DEAE paper chromatography and their subsequent digestion by venom phosphodiesterase (which initiates hydrolysis at the 3' terminus) results in the release of those nucleotides 3' to the dimer, since this exonuclease will not proceed beyond the dimer.

Exonucleolytic digestion by bovine spleen phosphodiesterase, which initiates hydrolysis at the 5′ terminus, releases those nucleotides located 5′ to the dimer. These data show that the majority of the nucleotides are located 3' to the dimer, and very few, if any, nucleotides exist on the 5′ incision side of the pyrimidine dimer. Such results substantiate those earlier observations in which denatured incised DNA was shown to be refractory to hydrolysis by spleen phosphodiesterases, indicating that the initial break is probably near or adjacent to the pyrimidine dimer.

PrcA has been purified to homogeneity from crude extracts of A. variabilis by ammonium sulfate precipitation followed by DEAE-cellulose chromatography and phenyl-Sepharose chromatography. Also, active recombinant PrcA was expressed in E. coli.

Recombinant HreP was expressed in E. coli with a C-terminal His6 tag and affinity purified by use of a Ni-nitriloacetic acid agarose column.

Purification to homogeneity of the mature protease was not achieved, as the preparations always contained unprocessed HreP and the processed propeptide in association with the mature protease. For more info visit us at https://biophoretics.com