Murein hydrolases in the envelope of Escherichia coli. Properties in situ and solubilization from the envelope.

Abstract

Properties of murein hydrolases, assumed to play an essential role in bacterial morphogenesis, are described. Evidence is presented that in the intact cell these enzymes are prevented from uncontrolled reaction. It is shown that the “barrier” between the enzymes and their substrate sacculus, a shape‐maintaining macromolecule within the cell envelope, can be artificially broken. Assay systems to measure murein hydrolase activity in the intact cell, in isolated cell envelopes and after solubilization are described. A combination of Triton X‐100 and sodium chloride is shown to liberate membrane‐bound hydrolases effectively.