Abstract
Microsomes and preparations of ribonucleoprotein particles were extracted with O[degree]2N-HC1 and the amino acid composition of the proteins was determined. A portion of about 40% of the total protein could be extracted from purified ribosomes. The extracted proteins possessed 24% of basic and 18% of acidic amino acid residues. The principal_N-terminal groups found were alanine, proline, glycine and serine. There were marked differences in the proportions of alanine and glycine contained in the basic and the HC1 acid-insoluble proteins.