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. 
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241 Citations
Highly Influential Citations
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Background Citations
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Methods Citations
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241 Citations

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…

A comparison of the physical chemical properties of oxidized and reduced alkylated ribonuclease.

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.

The reductive cleavage of disulfide bonds and its application to problems of protein 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.
...

References

SHOWING 1-10 OF 11 REFERENCES

Studies on the gross structure, cross-linkages, and terminal sequences in ribonuclease.

Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease.

The activity of ribonuclease after digestion with carboxypeptidase.

The separation of N-2:4-dinitrophenly amino-acids on paper chromatograms.

Lemoigne, M. (1942). Ann. Ferment. 7, 1, 129. McDonald, E. J. (1946). Advance8 in Carbohydrate Chemi8try, 2, 253. New York: Academic Press. Miller, B. F. & Van Slyke, D. D. (1936). J. biol. Chem.…

Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials

Poly-L-cysteine

The Reduction of the Disulfide Bonds of Insulin

Techniques and Reagents for Paper Chromatography

Über Papierionophorese bei Spannungsgefällen von 50 Volt/cm

[Paper partition chromatography of dinitrophenyl amino acids].