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710 SULleHYDRYL GROUPS OF EGG ALBUMIN IN DIFFERENT DENATURING

When egg albumin is denatured there occurs a striking change in its SH groups. This change provides a clue to an understanding of the change in configuration of the egg albumin molecule that takes place during denaturation. A protein can be denatured by many different agents. This is a well known and important characteristic of protein denaturation. In the present investigation our purpose is to discover whether different denaturing agents liberate the same or different numbers of SH groups in egg albumin. The change in SH groups is readily observed. Native egg albumin does not give a color reaction with nitroprusside and does not reduce ferricyanide; denatured egg albumin gives the color with nitroprusside characteristic of SH groups and immediately reduces ferricyanide (4, 17). This change in the SH groups of egg albumin is an example of the general rule that certain groups in a protein become reactive as a result of denaturation. Other groups, in addition to sulfhydryl, become reactive when egg albumin is denatured. Some of these groups also reduce ferricyanide, though they require a more alkaline medium for their activity than do SH groups. These reducing groups are probably the phenolic groups of tyrosine (20). The SH groups of denatured egg.albumin react with iodoacetate (17). Other groups of denatured albumin react with iodoacetate (22). Some of these groups, as yet unidentified, do not react with iodoacetate while the protein is native. There are proteins (in striated muscle and the crystalline lens of the eye) in which, unlike egg albumin, some SH groups are reactive even while the proteins are in the native state. Even while native, these proteins give a color reaction with nitroprusside and reduce ferricyanide (19). In these proteins denaturation produces a marked increase in the number of reactive SH groups. In other proteins (the serum proteins of the horse, for example) no SH groups are detectable either before or after denaturation. 1 But in both native and denatured serum proteins disulfide (SINS)