Partial Purification and Characterization of the Proteins from the 40‐S Ribosomes of Artemia salina and Wheat Germ

Abstract

The proteins were extracted from purified 40-S ribosomes derived from wheat germ and Artemia salina and separated by carboxymethylcellulose ion-exchange chromatography. Approximately four proteins from Artemia and four proteins from wheat germ were separated in a state of high purity. All proteins were identified by co-electrophoresis using a two-dimensional polyacrylamide gel system. A total of 30 unique proteins were found for Artemia and 32 proteins for wheat. The molecular weights of all proteins were estimated by sodium dodecylsulfate gel electrophoresis. Assuming each protein to be present in one copy per 40-S ribosome, the total protein molecular weight was estimated to be 560,000 associated with Artemia 40-S particles and 550,000 associated with wheat germ 40-S ribosomes.