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Different routes for integral protein insertion into Ricinus communis protein-body and glyoxysome membranes

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Abstract

Total polyadenylated RNA from ripening or germinating Ricinus communis L. endosperm was translated in rabbit reticulocyte lysate in the absence or presence of canine pancreatic microsomes. The products were immunoprecipitated using antibodies raised againts Triton X-114-extracted integral membrane proteins of protein bodies or glyoxysomes. While the proteins of proteinbody membranes were found to insert co-translationally into added microsomes, this was not observed in the case of glyoxysomal proteins. This observation was confirmed using antibodies raised against a purified glyoxysome membrane protein, alkaline lipase. These results indicate that different routes exist for the insertion of membrane proteins into the two organelles. In both cases membrane-protein insertion does not appear to be accompanied by proteolytic processing.

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Abbreviations

anti-PB:

antiserum to integral protein-body membrane proteins

anti-G:

antiserum to integral glyoxysomal membrane proteins

anti-L:

antiserum to alkaline lipase

ER:

endoplasmic reticulum

Mr :

relative molecular mass

mRNA:

poly(A)-rich messenger RNA

PAGE:

polyacrylamide gel electrophoresis

poly(A):

polyadenylic acid

SDS:

sodium dodecyl sulphate

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Halpin, C., Conder, M.J. & Lord, J.M. Different routes for integral protein insertion into Ricinus communis protein-body and glyoxysome membranes. Planta 179, 331–339 (1989). https://doi.org/10.1007/BF00391078

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  • DOI: https://doi.org/10.1007/BF00391078

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