By M. L.; Edsall, John T. (Eds) Anson
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Dakin’s widely used method of butanol extraction for the separation of monoamino-monocarboxylic acids from the rest has been shown not to be very specific (259, 260). The determination of the partition coefficients for a number of amino acids by England and Cohn (261) suggested, however, that with a suitable chromatographic technique many of the amino acids should be readily separable (cf. 262). Leland and Foster (263) by butanol extraction have estimated thyroxine and diiodotyrosine in thyroid glands.
Two dimensional chromatogram of a wool hydrolyzate First run with collidinc. Second run with henol. Quantity of protein used: 300 rg. The proline spot is a strong yellow color, gut does not show well in thc photograph. spots has not yet been found, but by a suitable choice of solvents any desired amino acid may be so obtained. Collidine, phenol, n-butanol and brnzyl alcohol are among the most useful solvents. The quantity of material required is remarkably small. 4 mg. Df protein is required for each 2-dimensional sheet and less for a l-dimensional experiment.
Rossouw and Wilken-Jorden (374) precipitated cysteine as its cuprous mercaptide with Cu~Cl2from ‘dirty’ hydrolyzates and decomposed the mercaptide before determining the cysteine colorimetrically. They were the first to notice that, as with glutathione (374a), the cuprous compound by itself is capable of reducing cystine to cysteine (cf. 375). Graff, et al. (376) employed Zn for the reduction, precipitated with CuzO, and estimated cyst(e)ine by N and S determinations (which were equivalent) on the mercaptide precipitate.