FIG. 3.

Limited proteolysis of purified MalK variants. Mutant proteins were digested with trypsin at a concentration of 48:1 (by weight) in the absence or presence of ATP. Samples were withdrawn at the indicated times and subsequently analyzed by immunoblotting as described previously (18). (A) Wild type, prepared according to reference 16; (B) L86F mutant; (C) E306K mutant. The relative positions of the previously recognized major cleavage products (T1 to T4) (18) are indicated. Fragments T2 and T3 were not separated under the conditions used here. Lane 1, undigested control. Results from representative experiments are shown.