Effects of sodium chloride concentration on solubility and electrophoretic characteristics of protein from the eye lens nucleus in a yellowfin tuna ( thunnus albacares) and in a desert wood rat ( Neotoma lepida)

Abstract

1. 1. A medium was sought which would extract from the eye lens nucleus all classes of proteins; albumins, euglobulins and pseudoglobulins. 2. 2. Cellulose acetate electrophoresis was performed on distilled water extracts and on saline extracts of thirty-three pieces of lens nucleus from a Yellowfin tuna, and of five pieces of lens nucleus from a desert wood rat. 3. 3. The protein patterns revealed that a 0·018 g% saline solution extracts both albumins and globulins, and produces no deleterious “salt effects”. The patterns also demonstrated that stronger saline solutions (e.g. physiological saline solution) produce simpler patterns due to the fusion of some proteins into single bands and the exclusion of others from solution. 4. 4. Of the various extracting fluids studied, the most effective for nuclear lens proteins, is 0·018 g% saline solution. Extracts prepared with this solution contain a total salt concentration of approximately 0·030 g% due to the presence of sodium chloride in the lens.