On a Phosphoprotein Isolated from Trout Egg
- 1 March 1963
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 53 (3), 242-243
- https://doi.org/10.1093/oxfordjournals.jbchem.a127686
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.Keywords
This publication has 3 references indexed in Scilit:
- Chemical Composition of the Egg-Yolk LipoproteinsThe Journal of Biochemistry, 1962
- PREPARATION AND CHARACTERIZATION OF PHOSVITIN FROM HEN EGG YOLKCanadian Journal of Biochemistry and Physiology, 1958
- AMINO ACID COMPOSITION OF EGG PROTEINSJournal of Biological Chemistry, 1950