Abstract
Abstract 1. The serum from unpreserved rubber (Hevea brasiliensis) latex contains seven electrophoretically distinct protein components. The proteins from whole serum originating in Sumatra and Florida give very similar results in electrophoresis experiments. 2. The relationship between electrophoretic mobility and pH has been determined for five of the seven protein components of unpreserved total latex serum. The results are considerably different from those reported by workers with ammonia-preserved latex, and tend to clarify observed differences in the stability behavior of unpreserved and preserved latex. 3. Ammonia-preservation treatment rapidly alters the electrophoretic behavior of the native protein components of latex serum and reduces the number of resolvable components from seven to two. 4. The preparation of dry latex protein from rubber-free latex serum can be accomplished by the vacuum sublimation of frozen serum. This process does not appear to produce important changes in the electrophoretic properties of the total serum proteins. 5. Minor modifications of the electrodes and of the standard illumination system in the electrophoresis apparatus are described.
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