%0 Journal Article
%A Meyer, David I.
%A Dobberstein, Bernhard
%D 1980
%F heidok:8481
%J THE JOURNAL OF CELL BIOLOGY 
%P 503-508
%R 10.11588/heidok.00008481
%T Identification and Characterization of a Membrane Component Essential for the Translocation of Nascent Proteins across the Membrane of the Endoplasmic Reticulum
%U https://archiv.ub.uni-heidelberg.de/volltextserver/8481/
%V 87
%X When rough microsomes are subjected to limited proteolysis and high salt, a soluble fraction can be separated from the membrane . Neither fraction alone is capable of vectorially translocating nascent peptides . When the soluble extract is recombined with the residual membrane fraction, translocating activity is restored . Standard biochemical techniques were used to identify and characterize the active component derived by treating rough microsomes with elastase and high salt. The active factor is a peptide fragment with an apparent molecular weight of 60,000. It represents the cytoplasmic domain of a larger membrane protein. The fragment is basic and has at least one accessible sulfhydryl group. These characteristics facilitated its purification and identification as a membrane component required for translocation of nascent peptides across microsomal membranes.