Control of an affinity purification procedure using a thermal biosensor
- 5 October 1990
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 36 (7), 723-726
- https://doi.org/10.1002/bit.260360710
Abstract
Lactate dehydrogenase (LDH) was recovered from a solution by affinity binding to an N6-(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.This publication has 6 references indexed in Scilit:
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