Extraordinary stability of the receptor of bacteriophage lambda.

The phage lambda receptor, previously shown to be a major outer membrane protein of Mr = 47 000 in maltose-grown Escherichia coli K12 (Braun, V. and Krieger-Brauer, H.J. (1977) Biochim. Biophys. Acta 469, 89--98), was found to be unusually resistant against the denaturants sodium dodecyl sulfate, urea and guanidine hydrochloride. A new isolation procedure for active phage lambda receptor, based on its resistance against pronase and hot sodium dodecyl sulfate, is described. The electrophoretic mobility of phage lambda receptor in sodium dodecyl sulfate polyacrylamide gels is abnormal even after heating in 2% sodium dodecyl sulfate, as is demonstrated by a Ferguson analysis. Phage lambda receptor in its active form sediments with a Svedberg constant of 8.4 +/- 0.4, which indicates an oligomeric structure of the phage lambda receptor.