The expression of several functional properties of the products of the bfe and tonB genes in Escherichia coli was measured after the specific termination of the synthesis of the products of these genes. This was accomplished by the use of a temperature-sensitive amber suppressor mutation, which allowed control, by manipulation of the growth temperature, of the level of product formed from suppressible mutant alleles of the bfe or tonB gene. The bfe product is an outer membrane receptor protein for vitamin B12, the E-colicins, and bacteriophage BF23. The identity of the tonB product is unknown, but it is necessary for a subsequent step of uptake of vitamin B12, iron chelates, all of the group B colicins, and bacteriophages T1 and phi 80. Results from a different experimental system had shown that the termination of expression of the bfe locus was rapidly followed by loss of sensitivity to colicins E2 and E3 and, subsequently, to bacteriophage BF23. This was confirmed with this experimental system. Receptors that were no longer functional for colicin or phage uptake remained fully effective for B12 uptake, showing that receptors are stable on the cell surface. This supports previous contentions for the presence of different functional states for colicin receptors. The functional properties of the tonB product, measured by B12 uptake or sensitivity to the group B colicin D, were unstable, declining extensively after cessation of its synthesis.