[Investigation of protease - inhibitor complex activity in the grain endosperm of Novosadska rana 2 wheat variety]
1985
Halasi, R. | Adamov, I. (Prirodno-matematicki fakultet, Novi Sad (Yugoslavia). Institut za hemiju)
In this research protease and inhibitor are isolated from grain endosperm of the wheat variety Novosadska rana, their activity is investigated and their homogeny examined by electrophoresis over polyacrylamide gel. The following was found: The complex protease-inhibitor was separated successfully in the acid medium of pH=4.5. Preparations of protease and inhibitor were isolated and purified from endosperm of the grain by modified methods. Purification was performed by settling with ammonium sulfate and with various solutions of trichloracetic acid. Enzyme activity of protease was 0.0045 EU and its specific activity was 0.01 EU/mg of protease. Activity of inhibitor in a mg of proteins of the inhibitor inducing a 100% inhibition of 1 mg of protease preparation was calculated. This activity was 2.11. There are 2 protease isoenzymes. Inhibitor consists of 2 different proteins. A weak activity of inhibitor was found, which can be explained by the reduction of inhibition during germination.
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