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Symmetrization of ArHgX with EDTA and NH3 24 hr at room temp. in aq. or org.-aq. mixts. gave 40-95% Ar2Hg (Ar = p-Br-, p-Cl-, p-AcNH-, p-NHMe-, Me, p-Et2N-, p-Me2N-, p-MeOC6H4; Ph; m-xylyl, pseudocumyl, pentamethylphenyl, duryl, isoduryl, mesityl, and $\alpha$-naphthyl). Other nucleophiles (e.g. BuNH2) were as effective as NH3, but EDTA was the best chelating agent. [on SciFinder(R)]

A high yield recyclization and pollution free process for the manuf. of diarylmercury compds. is described. The new process enables saving of starting materials and recovery of Hg. [on SciFinder(R)]

Treatment of 4 compds. of the type Ar(HgX)2 and of poly[4-(acetoxymercurio)styrene] with EDTA tetra-Na salt [64-02-8] and NH3 [7664-41-7] resulted in symmetrization and polymn. of the monomers and crosslinking of the polystyrene [9003-53-6] by Hg [7439-97-6]. E.g., 2,5-bis(chloromercurio)thiophene gave poly(mercurio-2,5-thiophenediyl) [57715-35-2]. [on SciFinder(R)]

PhHgOAc is converted into Ph2Hg via a symmetrization process, in the absence of an auxiliary ligand, at 6.5≥pH\textgreater4.0. Arylmercuric salts, in which the arom. rings contain more than 1 electron donating group, symmetrize in the absence of an auxiliary ligand at a basic pH. Both processes proceed in water or in mixts. of org. solvents and water. The factors influencing the symmetrization at different pH values are discussed. [on SciFinder(R)]

Asymmetrical diarylmercury compds., e.g. p-MeOC6H4HgC6H4NMe2-p, were produced together with sym. products via a symmetrization process. The asym. products could not be isolated from the reaction mixt. and their existence was indicated through different analyses (m.p., IR, PMR, mass spectra, elemental analysis and DTA). The asym. products are unstable and disproportionate into two sym. compds. at elevated temps., and in org. solvents even at room temp. [on SciFinder(R)]

The mechanism for the symmetrization of arylmercuric salts in the presence of chelating agents includes 3 main steps: (i) dissocn. of the arylmercuric salt; (ii) formation of a reactive complex between the ionized arylmercuric salt and the chelating agent; (iii) an electrophilic substitution at a C-Hg bond via a 2-electron, 3-center bond type transition state. The effect of chelating agents on the reactions of PhHgOAc with piperidine, BuNH2, or CNS- to give Ph2Hg and of m-MeC6H4HgOAc with tetra-Na ethylenediaminetetraacetate to give (m-MeC6H4)2Hg was discussed. [on SciFinder(R)]

The lysis of group A streptococci by muramidases of Streptomyces albus is strongly inhibited by human, rabbit, and calf serum as well as by human synovial fluids and pus. Rabbit antisera to heat-killed streptococci were no more inhibitory to the lysis of the streptococci by the lytic enzyme than normal rabbit serum. The results indicate that muramidases of S. albus will not be useful for the in vivo treatment of chronic granulomatous lesions which had been induced by insoluble cell wall components of streptococci.

The lysis of 14C-labeled bacteria by hydrolases of human and rabbit leukocytes was studied in vitro. While Staphylococcus albus, Streptococcus faecalis, and Streptococcus mutans were highly susceptible to lysis, Staphylococcus auresus was intermediate in its susecptibility to lysis by the leukocyte enzymes. Group A Streptococcus, Listeria monocytogenes, Shigella flexneri, Escherichia coli, and Mycobacterium smegmatis were very resistant to degradation by these enzymes. The lytic activity of leukocyte lysates from human and rabbit blood was probably due to acid hydrolases of polymorphonuclear leukocytes. Extracts of human blood monocytes and of rabbit peritoneal and lung macrophages were less lytic for the bacteria tested. Lymphocytes and platelet extracts were not bacteriolytic. The lytic effect of the leukocyte lysates was not inhibited by KCN or sodium azide, but was abolished to a large extent by cationic polyelectrolytes such as protamine sulfate, histone and leukocyte cationic proteins, and poly-lysine, as well as by the anionic polyelectrolytes such as heparin, chondroitin sulfate, DNA, carrageenin, alginate sulfate, dextran sulfate, and ploy-L-glutamic acid. Other potent inhibitors of bacteriolysis were trypan blue, congo red, phosphatidic acid, normal immunoglobulins, and components of streptococcal cell wall.

Acid hydrolases of human blood leukocytes are highly lytic toStaph. albus, Staph. aureus, andStrep. faecalis. On the other hand, group A and viridans streptococci, encapsulated staphylococci, a variety of Gramnegative rods, andMyc. smegmatis are highly resistant to lysis by leukocyte extracts. The lytic effect of the leukocyte extracts can be mimicked by an artificial "cocktail" which contains crude trypsin, lysolecithin, phospholipase C, and lysozyme. This enzyme mixture is lytic to certain Gram-negative bacteria and encapsulated staphylococci which are resistant to lysis by leukocyte enzymes. Both the leukocyte lysates and the artificial cocktail are more lytic to bacteria harvested from the logarithmic phase of growth than to older cells.Staph. albus andStrep. faecalis, which are not lysed to any appreciable extent by extracts of rabbit intestines, lymphocytes, and platelets, undergo extensive lysis upon the addition of lysozyme, indicating that these cells contain preparatory prolytic agents which are activated by lysozyme. On the other hand, the lysis ofStaph. aureus by extracts of all these cells is less dependent upon lysozyme, indicating that other non-lysozyme-dependent lytic factors are involved in the lysis of this microorganism by certain tissue extracts. It is suggested that the resistance to lysis by leukocyte enzymes of bacterial cell-wall constituents may contribute to the pathogenesis of chronic sequellae, and that artificial enzyme cocktails be used for in vivo treatment of certain chronic inflammatory processes induced by bacteria.

Lysis of(14)C-labeledStaph. aureus by human blood leukocyte lysates, by extracts of rabbit small intestines and pancreas, and by the "cocktail" of enzymes (containing trypsin, lysolecithin, and lysozyme) is strongly inhibited by anionic polyelectrolytes (e.g., heparin, chondroitin sulfate, liquoid (polyanethole sulfonic acid), and DNA). Most of the lytic agents employed were inhibited by cationic polyelectrolytes (e.g., histone, protamin sulfate and polylysin), as well as by gold thiomalate, normal human serum, synovial fluids obtained from patients with knee-joint trauma, extracts of coffee, tea, and cocoa, Ultracorten- and Dexamethasone. On the other hand, some antiinflammatory agents tested (e.g., indomethacin, aspirin, hydrocortisone acetate and succinate, and prednisolone acetate and tributyl acetate) were not inhibitory. All the cationic polyelectrolytes employed and liquoid were also strong inhibitors of lysozyme. Since mixtures of cationic and anionic polyelectrolytes at equimolar concentrations failed to inhibit bacteriolysis, it is postulated that the balance between charged macromolecular substances, which are likely to accumulate in inflammatory foci, may determine the fate of cellular components of bacteria in inflamed tissues. The possible role played by lysosomal enzymes and by tissue inhibitors in tissue damage and in the survival of bacteria in chronic inflammatory lesions is discussed.

THE DETERMINATION of antistrep- tolysin 0 (ASO) in patients’ sera is most commonly performed as an aid in the diag- nosis of streptococcal infection and their sequelae.’ However, because of the differences in immune responses to a variety of streptococcal exoproducts in rheumatic fever and glomerulonephritis, it is advantageous to measure the level of more than one antis trep tococcal antibody, particularly in patients with low or borderline ASO levels. 2.3 The recently developed streptozyme test (A-STZ)l is a two-minute slide hemagglutina- tion procedure which quantitatively meas- ures multiple antibodies to streptococcal exracellular products. The reagents are sheep red blood cells sensitized simultaneously with streptolysin 0 (SLO), deoxyribonuclease B (DNase B), hyaluronidase (H), streptokinase (SK), and nicotinamide adenine dinucleotide glycohydrolase (NADG). A good correlation betweenA-STZandASOinseraofrheumatic fever patients has been demonstrated. In a comparative study’ of the STZ test with titers obtained with three of the antibody tests, ASO, ADNase B, and AH, the useful- ness of the streptozyme test for laboratories which perform only the ASO test has been demonstrated. Similar conclusions were drawn in a comparative study in our laboratory. his report deals with three main topics: 1) the streptozyme studies done in our laboratories on four of human categories sera: control group, acute pyodermal ne- tients and acute rheumatic fever patients; 2) the reproducibility and specificity of the streptozyme test; and 3) the development of ASTZ in rabbits immunized with nonviable and viable streptococci.