Cereal Chem 47:5 - 11.  |  VIEW ARTICLE
Purification and Partial Characterization of a Major Globulin from Rice Endosperm.

D. F. Houston and A. Mohammad. Copyright 1970 by the American Association of Cereal Chemists, Inc. 

Albumins and globulins were extracted from rice flour with 5% sodium chloride solution. A major globulin component was purified by ammonium sulfate precipitation, repeated isoelectric precipitations, and gel- filtration chromatography. Progress was monitored by starch-gel electrophoresis. The purified globulin component migrates as a single compound in free-film and starch-gel electrophoresis, in column chromatography, and in ultracentrifugation. In the presence of urea it apparently dissociates into two portions which recombine when urea is removed. It shows no amylase activity, contains 18.1% nitrogen, has high glutamic acid and arginine content, moderately high serine, tyrosine, cystine, and methionine content, about 1% tryptophan, and essentially no lysine or histidine. Molecular weight estimated by Sephadex chromatography is about 25,500, and calculated from amino-acid content is 25,330. It has a sedimentation constant of 1.6S and calculated specific volume of 0.706.