Document Type



The solubilities of TlCl, TlCNS, and Tl2SO4, were determined in solutions of egg albumin at 25°C. The Tl+ was titrated to Tl+++ with standard KI03 using the ICl endpoint. The albumin concentration was determined by a modified Kjeldahl method. The pH of each solution was obtained with a glass electrode using M/20 potassium acid phthalate as a standard (pH= 3.97). In solutions of egg albumin dialyzed free of chlorides and sulphates and adjusted to a pH of 3.3 it was found that the greater the albumin concentration the greater was the amount of dissolved salt per 1000 g. of water. In albumin solutions at a pH of about 6 and to which no acid had been added a similar phenomenon was observed except that at small albumin concentrations the solubility of Tl2SO4 was less than in pure water. In dilute isoelectric albumin solutions all three salts studied were less soluble per 1000 g. of water than in pure water. These curves passed through a minimum and in some of the more concentrated albumin solutions the solubility became greater than in pure water. The valence and extent of hydration of the albumin cation was estimated from the solubility of TlCl at a pH of 3.3.

Publication Date


Journal Title

Proceedings of the Iowa Academy of Science





First Page


Last Page



©1939 Iowa Academy of Science, Inc.



File Format




To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.