Reductive cleavage of disulfide bridges in ribonuclease.

@article{Sela1957ReductiveCO,
  title={Reductive cleavage of disulfide bridges in ribonuclease.},
  author={Michael N. Sela and Frederick H. White and Christian B. Anfinsen},
  journal={Science},
  year={1957},
  volume={125 3250},
  pages={
          691-2
        }
}
This article was the first of many studies that were generally concerned with the eventual total synthesis of the protein. It contained several original observations that would lead to the conclusion that the refolding of the ribonuclease molecule after full denaturation by reductive cleavage of its four disulfide bonds required that only one of the one hundred five possible pairings of eight sulfhydryl groups to form four disulfide linkages take place. 

SOME RELATIONSHIPS OF STRUCTURE TO FUNCTION IN RIBONUCLEASE

This study by White and Anfinsen on the renaturation of fully denatured ribonuclease, or RNase, required subsequent supporting investigations to establish what came to be called the "thermodynamic

IMMUNOCHEMICAL REACTIONS INVOLVING RIBONUCLEASE *

This paper summarizes chemical and enzymic experiments that have delineated some of the groups concerned with the reaction between RNase and its antibody.

Protection of Thiols

This chapter will deal primarily with the protection of cysteine residues and the means by which cysteined residues may be deblocked and converted to cystine or retained as the thiol.

The role of disulfide bonds in the protein structure. Conformational studies on reduced ribonuclease and lysozyme.

The results obtained indicate a large disorganization of the native molecules when all disulfide bridges are broken even if in both fully reduced proteins there appears to be some residual non-covalent structure.

Cleavage of one specific disulfide bond in papain.

THE RELATION OF STRUCTURE TO ENZYMATIC ACTIVITY IN RIBONUCLEASE *

The methods of assaying for RNase and an active fragment of KNase containing an active center (if it exists) are improved, and questions relating the structure of the ribonuclease molecule to its enzymatic activity are attempted.

The reformation of disulfide bridges in proteins.

The reduction of protein disulfide bonds in the absence of denaturants.

  • T. BewleyC. Li
  • Biology, Chemistry
    International journal of protein research
  • 1969
The ability of dithiothreitol to effect the reduction of the disulfide bonds in five proteins under mild conditions and in the absence of denaturant has been examined and Lysozyme, prolactin, and insulin appeared to be quantitatively reduced.
...

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