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. 2001 May;183(9):2774–2778. doi: 10.1128/JB.183.9.2774-2778.2001

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
a

The data were obtained with 16.9 g of wet cell paste. 

b

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%.