The Effect of Egg Albumin on the Solubility of Thallous Salts at 25 C

Authors

W. G. Eversole, State University of IowaFollow
Carold F. Bjork, State University of Iowa

Document Type

Research

Abstract

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

1939

Journal Title

Proceedings of the Iowa Academy of Science

Volume

46

Issue

1

First Page

200

Last Page

201

Copyright

©1939 Iowa Academy of Science, Inc.

Language

en

File Format

application/pdf

Recommended Citation

Eversole, W. G. and Bjork, Carold F. (1939) "The Effect of Egg Albumin on the Solubility of Thallous Salts at 25 C," Proceedings of the Iowa Academy of Science, 46(1), 200-201.
Available at: https://scholarworks.uni.edu/pias/vol46/iss1/38