Localization of the lactose permease protein(s) in the E. coli envelope. |
| |
Authors: | M Villarejo C Ping |
| |
Affiliation: | Department of Biochemistry and Biophysics University of California Davis, California 95616 USA |
| |
Abstract: | The amino acid double labeling technique was used to identify and localize membrane-bound lactose operon proteins in . Both the “M” protein, thought to be the gene product, and a polypeptide of MW ~15,000 appeared in the membrane following operon induction. The amounts of these two proteins were approximately equal.The inner and outer membrane layers of the cell envelope were separated by sucrose density gradient centrifugation or by selective solubilization of inner membranes with the detergent Sarkosyl. When gentle lysis conditions were employed to prepare membrane vesicles, both induced proteins fractionated with the inner membrane. However, the “M” protein was more easily randomized in the envelope structure by sonication than the 15,000 dalton component or an inner membrane marker enzyme. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|