Sulfhydryl and Disulfide Groups of Proteins


In a previous paper methods were described for estimation of the sulfhydryl (SH) and disulfide (S-S) groups of proteins. I t was shown that in a denatured but unhydrolyzed protein the number of groups detectable is the same as that found in the hydrolyzed protein (Mirsky and Anson, 1934-35)3 With the same methods, applicable to native as well as to denatured proteins, it is found that in some native proteins no SH and S-S groups can be detected, while in others a fraction of the number present when the protein is denatured can be detected. In this paper it is shown that when a protein is partially denatured, that is when part of it is converted into a form insoluble under conditions under which the native protein is soluble, the insoluble fraction has the number of reactive SH and S-S groups characteristic of completely denatured protein, whereas the soluble fraction has the number characteristic of protein which has not been denatured at all. When denaturation is reversed, when insoluble protein is converted into soluble protein, groups which have been detectable are so no longer. In the interfacial coagulation of a protein, that is, when a film of insoluble protein forms at the surface of a protein solution, groups appear, the number detectable being the same as that found in the hydrolyzed protein. When a protein is coagulated by irradiation with ultraviolet


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@article{Mirsky1936SulfhydrylAD, title={Sulfhydryl and Disulfide Groups of Proteins}, author={Alfred E . Mirsky and Man-Yee L. Anson}, journal={The Journal of General Physiology}, year={1936}, volume={19}, pages={427 - 438} }