Control of an affinity purification procedure using a thermal biosensor.
Lactate dehydrogenase (LDH) was recovered from a solution by affinity binding to an N(6)-(6-aminohexyl)-AMP-Sepharose gel. An enzyme thermistor unit was employed to continously measure the activity of the unbound LDH. The enzyme activity signal from the enzyme thermistor was used in a PID controller to regulate the addition of AMP-Sepharose gel to the LDH solution. In another type of experiment, a desktop computer was utilized to control the addition of the adsorbent. Both systems worked satisfactorily, and enabled a rapid and accurate assessment of correct addition of adsorbent.
Flygare
L
L
Pure and Applied Biochemistry, Lund University, Box 124, S-221 00 Lund, Sweden.
Larsson
P O
PO
Danielsson
B
B