Five monoclonal antibodies (MoAbs) to gag proteins of HIV-1 were prepared in mice. Western blot analyses showed that three clones recognized p24 and the other two p17. Among the three MoAbs recognizing p24, all recognized two of three strains of HIV-2. The spectra of reactions to SIV [AGM] of these MoAbs against p24 were different from one to another; K3-24 recognized all four strains of SIV [AGM], L6-24 three of them, and K5-24 none of them. Of the two MoAbs recognizing p17, K7-17 recognized two of the three strains of HIV-2 but not any SIV [AGM] strain, and the other clone, L14-17 recognized none of analogous proteins of HIV-2 nor of SN [AGM] . These results demonstrate that the gag proteins of HIV-2 and SIV [AGM] share some common epitopes with those of HIV-1 which are heterogenic in some degree among the different isolates.

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In a whole cell assay system with p-nitrophenyl phosphate as substrate, strains of Pseudomonas pseudomallei showed a two-peak pattern in pH activity curve of acid phosphatase, suggesting the presence of two enzyme components different in pH optimum (4.2 and 5.2) . The component of 5.2 pH optimum was detected in the outer membrane fraction and the activity was resistant to heating at 70 C for 30 min. The other component of 4.2 pH optimum was heat-labile. No substantial difference was observed in the enzymatic activity between R and S type colonies.

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A study was made on the growth and survival of Pseudomonas pseudomallei in culture environments differing in nutrients, initial pH, and aeration, in comparison with Pseudomonas cepacia and Pseudomonas aeruginosa. The observations led us to a view that P. pseudomallei has the highest adaptability to acidic environments among the three species. Unlike the other species, it grew in heart infusion broth of initial pH 4.5 under aeration and survived keeping a high level (10⁹ per ml) of viable counts for as long as 30 days. This sort of adaptation was found to be more evident in the media of poor nutrition and under limited aeration.

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Polyclonal and monoclonal antibodies to platelet-activating factor (PAF) were produced, by use of colloidal gold as the hapten carrier. These polyclonal (R88-09) and monoclonal (602 B11) antibodies both reacted with PAF, lysoplatelet-activating factor (lyso PAF), and L-α-lysophosphatidylcholine, palmitoyl (lyso PCP), but did not react with phosphorylcholine chloride (PCC) . Their affinities were higher for PAF than lyso PAF and lyso PCP.

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