TABLE 1.
Purification of dephospho-CoA kinase from C. ammoniagenesa
Purification step | Protein (mg) | Activity (U) | Sp act (U/mg) | Yield (%) | Purification (fold) |
---|---|---|---|---|---|
Crude extract | 1,600 | 3.6b | 0.0023 | ||
DEAE Sepharose | 270 | 3.6 | 0.013 | 100 | 5.7 |
Red A agarose | 1.2 | 3.0 | 2.5 | 83 | 1,100 |
Q Sepharose | 0.2 | 1.3 | 6.5 | 36 | 2,800 |
The data were obtained with 16.9 g of wet cell paste.
Dephospho-CoA kinase activity could not be measured in the crude extract because of high background activity. The yield of DEAE Sepharose activity was thus assumed to be 100%.