On the Heterogeneity and Purification of Commercial Trypsin Preparations.
- 1 January 1966
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 20 (1), 175-182
- https://doi.org/10.3891/acta.chem.scand.20-0175
Abstract
Three commercial preparations of crystalline trypsin were found to differ from one another in their specific activity as well as in the ratio between their activity and the STI [soybean trypsin inhibitor]-binding capacity. On gel filtration the trypsin preparations separated into 2 esterolytically active components differing from each other in molecular weight, activity in relation to STI-binding capacity and electrophoretic mobility. On electrophoresis in agarose the trypsin preparations separated into several enzymatically active fractions, differing in activity from fraction to fraction and from one preparation to another.This publication has 7 references indexed in Scilit:
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