The reactivity of the disulphide bonds of purified proteins in relationship to primary structure.

  title={The reactivity of the disulphide bonds of purified proteins in relationship to primary structure.},
  author={B. E. Davidson and F. J. R. Hird},
  journal={The Biochemical journal},
  volume={104 2},
1. With the aid of a coupled system involving glutathione reductase, the reaction of glutathione with the disulphide bonds of purified proteins has been studied. 2. Bovine serum albumin, conalbumin, lysozyme, trypsin inhibitors from egg white, lima bean and soya bean either did not react with glutathione or reacted only slightly. With these proteins reactivity was markedly increased by limited proteolysis. 3. Bovine and human gamma-globulins, fibrinogen and beta-lactoglobulin exhibited some… 

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Kinetic regime of dithiothreitol-induced aggregation of bovine serum albumin.


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