Abstract
There has been an outburst of renewed interest in the .beta.-lactam antibiotics in the last 5-6 yr. One of the main factors contributing to this was the introduction of the simple and powerful technique of sodium dodecyl sulfate electrophoresis for the identification of bacterial membrane components, penicillin binding proteins, that bind radioactive penicillin and most likely represent the primary biochemical targets of penicillin action in the bacterial cell. Application of this technique led to a remarkable number of novel observations that have substantially modified views of the mode of action of .beta.-lactam antibiotics.