Abstract
The interaction of sodium desoxyribosenucleate and bovine serum albumin in phosphate buffers has been studied under various conditions of pH, by the technique of light scattering. Interpretation of the experimental data in terms of the theories of light scattering from large molecules and multi-component systems has permitted the determination of the composition of soluble nucleoprotein complexes as well as their size and shape. There is no reaction at pH 7.47 and 6.46. At pH 5.51 and ionic strength 0.1, the nucleic acid binds 35% of its own weight of bovine serum albumin in a 1:1 mixture, that is, each molecule of nucleic acid on the average binds 11 ± 2 molecules of the protein. The nucleic acid undergoes no appreciable changes of shape upon reaction.
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