The histamine releasing properties of some agents used in textile industry.

The inflammatory effect of some compounds (polyglycolamines and polyglycolalcohols condensated with various number of ethylene oxide groups) used in textile industry were investigated as to their action on skin vascular permeability in rats and histamine release from rat peritoneal mast cells. The intradermal injection of tested agents caused the inflammatory skin reactions of various intensity depending on time, dose and chemical structure of agent used. It has been also shown that these properties of tested compounds were correlated with their histamine releasing activity and seemed to be dependent on their chemical structure, namely, the number of ethylene oxide groups in molecule. It is suggested that the histamine release induced by tested compounds is of cytotoxic nature since it depends neither on metabolic energy nor on extracellular calcium.

Effect of histamine on E and EAC rosettes formation of normal and leukemic human lymphocytes.

Histamine at 10(-6) M inhibited E and increased EAC rosette formation of normal human peripheral lymphocytes. Cimetidine at 10(-3) M prevented the decrease in number of E rosette-forming cells. In CLL no influence of Hi on both E and EAC rosette formation was detected. In the light of these findings the presence of histamine receptor on human normal and leukemic lymphocytes is discussed.

Determination of histaminase (diamine oxidase) activity by o-dianisidine test: interference of ceruloplasmin.

Until now o-dianisidine was used as an indicator substance in a test system for the determination of diamine oxidase. More recently, however, this substance was also used to measure ceruloplasmin activity. A study of the test principles revealed that o-dianisidine was the one denominator for both enzymes. As it was found for diamine oxidase the indicator was oxidized via peroxidase mediated H2O2 cleavage. Ceruloplasmin, however, oxidized o-dianisidine directly with resulting free radical formation. An addition of histamine dihydrochloride or putrescine dihydrochloride to an incubation mixture, containing ceruloplasmin as enzyme and o-dianisidine or p-phenylene-diamine as substrates, produced an activation of the enzyme, being more than 10-fold in the presence of 1 X 10(-2) M putrescine at pH 7.0. It was assumed that an allosteric effect of the dihydrochloride component might be responsible for this activation. When the activity of purified diamine oxidase was determined by the o-dianisidine test and by the isotope assay, a very good correlation between both methods was found. But, in a mixture of diamine oxidase and ceruloplasmin, no differentiation between the two enzymic activities by the o-dianisidine test was possible. This observation demonstrated an interference of ceruloplasmin when the o-dianisidine method was used for the determination of diamine oxidase activity. To apply our findings also in vivo the amine oxidase activity increasing in guinea-pig plasma during inflammation, was determined by the o-dianisidine test and by specific methods for some amine oxidase. Despite an enhanced oxidation of the o-dianisidine observed, only an increase of ceruloplasmin activity was found. It was concluded that ceruloplasmin had no 'histaminase activity' as has been assumed by other authors using the o-dianisidine test.