Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.

@article{Brocklehurst1981DifferencesIT,
  title={Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.},
  author={K. Brocklehurst and Baldev S. Baines and J. P. Malthouse},
  journal={The Biochemical journal},
  year={1981},
  volume={197 3},
  pages={
          739-46
        }
}
1. A rapid method of isolation of fully active actinidin, the cysteine proteinase from Actinidia chinensis (Chinese gooseberry or kiwifruit), by covalent chromatography, was devised. 2. The active centre of actinidin was investigated by using n-propyl 2-pyridyl disulphide, 4-(N-aminoethyl 2'-pyridyl disulphide)-7-nitrobenzo-2-oxa-1,3-diazole and 4-chloro-7-nitrobenzofurazan as reactivity probes. 3. The presence in actinidin in weakly acidic media of an interactive system containing a… Expand
Enzymatic properties, substrate specificities and pH-activity profiles of two kiwifruit proteases.
...
1
2
3
4
5
...