Membrane proteins synthesized by rabbit reticulocytes.
Intact rabbit reticulocyte cells synthesize two predominant species of polypeptides which are components of the cell plasma membrane. Previous work (Lodish, H. F. 1973. Proc. Natl. Acad. Sci. U. S. A. 70:1526-1530.) showed that these proteins were synthesized by polyribosomes not attached to membranes. We show here that both polypeptides are confined to the cytoplasmic surface of the cell membrane. These studies utilized iodination of whole cells and of membranes with lactoperoxidase, and digestion of whole cells and membranes with chymotrypsin, One of these proteins is synthesized as a precursor, and about 20-40 amino acids are removed after it is incorporated into the membrane, We discuss the probable sites of synthesis of these and other classes of membrane proteins.
D000818:Animals; D001798:Blood Proteins / Q000096:biosynthesis*; D002462:Cell Membrane / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D007457:Iodine Radioisotopes; D010544:Peroxidases; D011132:Polyribosomes / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*
D001798:Blood Proteins; D007457:Iodine Radioisotopes; D010544:Peroxidases; D002918:Chymotrypsin