TY  - JOUR
EP  - 508
A1  - Meyer, David I.
A1  - Dobberstein, Bernhard
UR  - https://archiv.ub.uni-heidelberg.de/volltextserver/8481/
N2  - 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.
AV  - public
Y1  - 1980///
TI  - Identification and Characterization of a Membrane Component Essential for the Translocation of Nascent Proteins across the Membrane of the Endoplasmic Reticulum
VL  - 87
SP  - 503
ID  - heidok8481
JF  - THE JOURNAL OF CELL BIOLOGY 
ER  -