In: THE JOURNAL OF CELL BIOLOGY , 87 (1980), pp. 503-508.
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.
|Journal or Publication Title:||THE JOURNAL OF CELL BIOLOGY|
|Date Deposited:||17. Jun 2008 17:01|
|Page Range:||pp. 503-508|
|Faculties / Institutes:||Service facilities > Center for Molecular Biology Heidelberg|
|Subjects:||570 Life sciences|
|Schriftenreihe ID:||Works by Bernhard Dobberstein|