By P. Alexander, H. P. Lundgren
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Additional info for A Laboratory Manual of Analytical Methods of Protein Chemistry. Volume 4
5. HgCl 2 has no special advantages over MeHgl for this estimation other than its ready availability in a pure form and the fact that the conditions for its use have been well established and described by Stricks et al. (1954). * The solution used here is NH4-SO3 "-urea * See footnote on page 38. 42 ANALYTICAL METHODS OF PROTEIN CHEMISTRY buffer (pH 9-2), made up as described in Section (a). This solution (10 ml) is added to the polarographic cell (Fig. 5) and purified N 2 gas is passed over the top of the solution for 10 min.
If w mg of the sample, added to v ml of MeHgl (5 x 10 ~~4) cause a reduction in the height of the polarographic wave from / blank to id, then the —SH content of the sample is : ■^^ *blank x - x 500 micromoles per g of sample, W where the weights may be expressed on a wet or dry basis, and id has been corrected for possible dilution. If a recording polarograph is not available, a manual one may be used. In this case, instead of plotting current-voltage curves, single current readings at —0-8 V are sufficient to measure / blank and id, although the precision is a little lower.
We have seen (Section III. (b) that among the products are such intermediate oxidation states as —SOS—, —S0 2 S, —S0 2 S0 2 —, —SOH, and —S0 2 H as well as —S0 3 H. When such proteins are completely hydrolysed in acid, the partially oxidized groups do not survive intact and are converted in varying yields to cysteic acid, cystine and cysteine. The interpretation of —SH and —SS— titration data on hydrolysates of partially-oxidized or irradiated proteins is too complex to attempt, without carrying out parallel estimations on the unhydrolysed proteins.
A Laboratory Manual of Analytical Methods of Protein Chemistry. Volume 4 by P. Alexander, H. P. Lundgren