| Autor: |
Santer, Melvin, Ruebush, Trenton K., Van Brunt, John, Oldmixon, Eben, Hess, Russell, Primakoff, Paul, Palade, Philip |
| Zdroj: |
Journal of Bacteriology; April 1968, Vol. 95 Issue: 4 p1355-1367, 13p |
| Abstrakt: |
Antibodies prepared against proteins from 50Sribosomes of Escherichia colialso reacted with the supernatant proteins of a cell-free extract of E. coliwhich was ribosome-free. A reaction of immunological identity (Ouchterlony tests) was demonstrated for one of these supernatant proteins and one protein found in 50Sribosomes. Isotope experiments involving a shift from 14C-leucine medium to 12C-leucine medium showed that these proteins are not formed by breakdown of ribosomes during the preparation of cell-free extracts, but instead represent a pool of ribosome protein which is utilized during growth. In shift experiments from 14C-leucine to 12C-leucine medium, the kinetics of disappearance of labeled supernatant ribosome proteins (as measured by reaction with antibody) indicated that half the pool is depleted in 0.1 generation time at 37 C in glucose-salts medium. The pool was also depleted under conditions of amino acid starvation of a “relaxed” strain which accumulated “relaxed” particles. Most, if not all, of the protein present in “relaxed” particles was derived from the pool. The pool represented about 3 to 4% of the total soluble proteins in the ribosome-free supernatant fluid of an E. coliextract. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
