Studies on lipin-protein complexes
- 1 January 1928
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 22 (3) , 800-810
- https://doi.org/10.1042/bj0220800
Abstract
When a mixture of lecithin and caseinogen is added to a series of lactate buffer solutions of pH between the iso-electric points of the substances, the % of precipitated lecithin increases regularly with increasing acidity of the solutions. When lecithin and caseinogen are added in widely differing proportions to the same buffer solution, the pH being again intermediate between the 2 iso-electric points, the % of lecithin in the precipitated complexes increases at first rapidly, then gradually, and ultimately very slowly with increases in the proportion of lipin. The existence of this range in which the composition of the precipitated complex varies but slightly with change in proportions of the constituents has led previous authors to assume the production of definite chemical compounds between lipins and proteins, but the whole behavior can be explained in terms of the mutual neutralization of charge and consequent precipitation of 2 oppositely charged colloids, the intensity of whose charge varies with the ph of the medium.This publication has 2 references indexed in Scilit:
- Observations on some Processes of Oxidation in Blood-serumBiochemical Journal, 1927
- The Apparent Formation of Euglobulin from Pseudo-Globulin and a Suggestion as to the Relationship between these two Proteins in SerumBiochemical Journal, 1914