Abstract
A method is described for establishing salting-out curves of proteins by means of spectrophotometrical measurements of their absorption in ultraviolet light of 2.750 A wave-length. The measurements are performed on the—suitably diluted—solutions of proteins in salt mixtures with increasing salt concentration, after removal of precipitated proteins. Several samples of horse serum and of pathological human serum have been examined by this method. Comparison of the results with those obtained by micro-Kjeldahl analysis shows a satisfactory agreement between both methods as regards the groups of protein constituents revealed, and also indicates their differences in aromatic amino acid composition. The advantages and disadvantages of the spectrophotometric method as compared to the Kjeldahl method are discussed. It is more rapid than the latter and useful for qualitative analysis of a protein mixture, but less suitable for quantitative evaluation of the results. It is especially convenient for work with ammonium sulphate.
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