The receptor for phage lambda in Escherichia coli was isolated by cholate extraction and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Protein bands corresponding to the monomer and the dimer were eluted from the gel and tested for their activity to inactivate phage lambda and to form pores in black lipid membranes. It was found that only the dimer inactivated phage lambda, whereas both the monomer and the dimer were active in forming pores. The pore characteristics were similar to those exhibited by the matrix protein (porin) (R. Benz, K. Janko, W. Boos, and P. Läuger, Biochim. Biophys. Acta 511:305--319, 1978). In comparison, the lambda receptor showed a somewhat higher degree of cation specificity, and its pore size was larger. Assuming that the thickness of the outer membrane is 7.5 nm and that the pore is an ideal hydrophilic channel, the pore diameter in vivo was estimated to be 1.6 nm for the lambda receptor and 1.2 nm for the matrix protein.

Osmotic shock fluid of Escherichia coli exhibited pore-fonming activity. This activity could be followed by an in vitro assay based on the conductivity increase for ions due to the presence of pores in black lipid membranes. The histogram (the distribution of conductivity increments in a single pore experiment) obtained with osmotic shock fluid from E. coli was identical to the histogram obtained by detergent-solubilized porin isolated from the outer membrane. The osmotic shock fluid from porin-negative mutants also exhibited pore activity, although the histogram and ion specificity were different from those of porin. Antibodies raised against detergent-solubilized porin were able to form precipitin lines by the Ouchterlony immunodiffusion technique when shock fluids, but not detergentsolubilized porin, were used. These antibodies prevented the formation of pores when shock fluids contained porin but not when shock fluids obtained from porinnegative mutants were used. Macroscopic membrane conductivity of shock fluids due to porin exhibited a concentration dependence, in contrast to detergentsolubilized porin. These results indicate that the hydrodynamic properties of periplasmic or "soluble" porin are different from those of the detergent-solubilized porin of the outer membrane. Periplasmic porin comprises about 0.7% of total protein in the osmotic shock fluid.

Paraquat dichloride (l,l'-dimethyI-4,4'-bipyridylium dichloride) induced the production of the hydrocarbon gases propane, ethane and ethylene in the xanthophycean microalga Burnilleriopsis filiforrnis. Formation of these gases was dependent on the light intensity and photosynthetic electron transport. Diquat dibromide (1 ,l'ethylene-2,2'-bipyridylium dibromide), having a higher midpoint potential than paraquat dichloride, induced an even higher evolution of the gases. A total lack of oxygen inhibited the production of gas, while a low oxygen concentration ( 4 6 % by volume) stimulated paraquat-induced gas formation. Culturing algae autotrophically, in a medium with a higher iron content, also increased the production of gases in the presence of the herbicide. Formation of these gases is an indication of the peroxidation of membrane lipids which, according to previous results, is correlated with a decrease of photosynthetic electron-transport activity.

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