Identification of ribophorins in rough microsomal membranes from different organs of several species

Eur J Biochem. 1982 May;124(1):217-22. doi: 10.1111/j.1432-1033.1982.tb05928.x.

Abstract

Microsomes prepared from several animal sources were analyzed for the presence of proteins corresponding to the ribophorins (I and II) which have been previously characterized in rat liver rough microsomes and appear to be involved in the binding of polysomes to endoplasmic reticulum membranes. In rough microsomal membranes from rat lacrimal gland, rabbit liver, dog and chicken pancreas, and mouse myeloma, ribophorin-like polypeptides with similar electrophoretic mobilities were detected by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. In all cases the polypeptides remained associated with sedimentable polysomes after solubilization of the microsomal membranes with nonionic detergents. Ribophorin-like polypeptides were absent from smooth microsomes. Antibodies raised against each rat liver ribophorin, purified by preparative sodium dodecyl sulfate/polyacrylamide gel electrophoresis, immunoprecipitated only the corresponding polypeptide, indicating no crossreactivity between ribophorins I and II. These antibodies also immunoprecipitated the homologous ribophorins found in microsomal preparations from other organs and species.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chickens
  • Dogs
  • Endoplasmic Reticulum / metabolism
  • Glycoproteins / isolation & purification*
  • Intracellular Membranes / analysis*
  • Lacrimal Apparatus / analysis
  • Male
  • Membrane Proteins / analysis*
  • Mice
  • Microsomes / analysis*
  • Microsomes, Liver / analysis
  • Myeloma Proteins / isolation & purification
  • Pancreas / analysis
  • Rabbits
  • Rats
  • Rats, Inbred Strains
  • Species Specificity

Substances

  • Glycoproteins
  • Membrane Proteins
  • Myeloma Proteins
  • ribophorin