The Assembly of a Structural Lipoprotein in the Envelope of Escherichia coli

摘要: Abstract A major envelope protein of Escherichia coli was found to exist in two different forms the envelope. One-third is covalently linked peptidoglycan (bound form) as by Braun and his co-workers. The remaining two-thirds are but not (free form). In contrast free form, bound form can only be solubilized 1% sodium dodecyl sulfate (SDS) after lysozyme treatment thus shows a slightly higher molecular weight than on SDS acrylamide gel electrophoresis because it has an attached fragment. When E. cells were pulse-labeled with [3H]- or [14C]arginine for 4 min, all radioactivity form. Chasing non-radioactive arginine showed that portion converted into ratio reached constant level chasing one doubling time. These results indicate first synthesized then It appears reaction between reversible there dynamic equilibrium conversion from inhibited chloramphenicol, amino acid starvation (arginine), carbonyl cyanide m-chlorophenylhydrazone.