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The article presents information on various research papers which will be published in the forthcoming issue of the "European Journal of Biochemistry". Some of the papers discusses are "Enzymatic Synthesis of Neolactotetraosylceramide by the N-Acctyllactosamine Synthase of Human Serum". "Rate of Transplantation and Kinetics of Processing of Newly Synthesized Molecules of Two Major Outer-Membrane Proteins, the OmpA and OmpF Proteins of Escherichia Coli," by the researchers I. Crowlesmith and K. Gamon.

Six monoclonal antibodies directed against the trimeric from of outer-membrane pore protein PhoE of Escherichia coli K-12 were isolated and characterized. All six antibodies bind to PhoE protein in intact cells and as isolated trimers, but not to dodecyl-sulphate-denatured monomers. Cross-reaction with the related pore proteins OmpF protein and OmpC protein was not observed. A hybrid pore protein in which the amino-terminal 74 amino acids of PhoE protein have been replaced by the corresponding part of OmpF protein is able to bind the six monoclonal antibodies. Five of the antibodies bind to the PhoE proteins of thirteen different Enterobacteriaceae when expressed in E. coli K-12, whereas the other antibody recognizes PhoE protein from nine of these strains. Four monoclonal antibodies are able to block adsorbtion of the PhoE-protein -specific phage TC45 to its receptor on whole cells. None of the antibodies has any effect on the uptake rate of the antibiotic cefsulodin through PhoE protein pores. Five antibodies are able to direct the complement-mediated killing of cell-surface-exposed epitopes whose specificity is determined by the carboxy-terminal 256 amino acids of PhoE protein. [ABSTRACT FROM AUTHOR]