Abstract
Rough and smooth microsomes were prepared from ascites tumor cells, rat liver, and bovine adrenal cortex. Proteolytic removal of the signal peptide in pre-placental lactogen and asparagine-linked glycosylation of the alpha subunit of chorionic gonadotropin by these fractions were examined in mRNA-dependent lysates from ascites cells. Both processing steps were performed by smooth microsomes, which was unexpected because it has been presumed that only rough microsomes contain components for ribosomal binding. Thus smooth microsomes are apparently capable of interacting with polysomes bearing secretory nascent chains, and cleavage and asparagine-linked glycosylation activities are present in both rough and smooth endoplasmic reticulum.
MeSH Terms
Adrenal Cortex/ultrastructure
Animals
Ascites/pathology
Cattle
Chorionic Gonadotropin/metabolism
Glycoproteins/metabolism
Hexosyltransferases/metabolism
Membrane Proteins/metabolism
Microsomes/metabolism
Microsomes, Liver/metabolism
Molecular Weight
Neoplasms, Experimental/ultrastructure
Placental Lactogen/metabolism
Protein Precursors/metabolism
Rats
Chemicals
Chorionic Gonadotropin
Glycoproteins
Membrane Proteins
Protein Precursors
Placental Lactogen
Hexosyltransferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bielinska M
Rogers G
Rucinsky T
Boime I
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