On a Phosphoprotein Isolated from Trout Egg

Abstract

Matured eggs of Salmo irideus were extracted by homogenizing with bicarbonate buffer, pH 9.8(ionic strength 0.2), and subjected to starch grain electrophoresis at pH 9.8(bicarbonate buffer, ionic strength of 0.2), which separated phosphoprotein, simple proteins, and lipoproteins in the descending order of mobility towards anode. Yield of the phosphoprotein was 6%. The phosphoprotein was homogeneous in ultra-centrifuge (1.9 [image] units) at pH 9.8, and contained 4% P and 14.8% N. Hydrolysis of the phosphoprotein by 6[image] HC1 yielded glycine, alanine, serine, asparagine, glutamic acid and an unidentified ninhydrin-pos. substance.