Acta microbiologica Academiae Scientiarum Hungaricae最新文献

{"title":"Sensitizing activity to egg protein of an A1PO4-adjuvant full-virus influenza vaccine.","authors":"G Nyerges, A Marton, S Korossy, I Vincze","doi":"","DOIUrl":"","url":null,"abstract":"The sensitizing activity to egg protein of an A1PO4-adjuvant purified and concentrated influenza-A vaccine was examined in animal experiments and in man. Intravenous injection of ovalbumin caused anaphylactic symptoms and/or fatal anaphylactic shock in prevaccinated guinea-pigs. Ovalbumin-specific antibodies detectable by the passive haemagglutination reaction (PHA) appeared in the blood serum of the vaccinated animals. Model experiments with purified ovalbumin suggested that 1 human dose of the vaccine contained egg protein in the range from 0.1 to 1 ng, and that the antigenic effect of the vaccine grew to more than 10(3)-fold by its adsorption to A1PO4 gel. Adults who in previous years had been immunized with similarly prepared influenza vaccine several times responded with mild reactions; symptoms suggestive of hyperergy did not occur, irrespective of the vaccination history. In the prevaccination serum sample of some vaccines, ovalbumin-specific PHA antibodies were found up to titres independent of the number of the previous immunizations. The concentration of the ovalbumin-specific antibodies of the IgE class was by several orders of magnitude lower in the postvaccination samples than in the serum of some patients hypersensitive to egg protein.","PeriodicalId":75387,"journal":{"name":"Acta microbiologica Academiae Scientiarum Hungaricae","volume":"29 4","pages":"245-53"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18201517","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Drug-receptor interaction on plasmid elimination by phenothiazines and imipramine in Escherichia coli. 药物受体相互作用对大肠杆菌中吩噻嗪和丙咪嗪质粒消除的影响。

Acta microbiologica Academiae Scientiarum Hungaricae Pub Date : 1982-01-01

J Molnár, Y Mándi, S Földeák

{"title":"Drug-receptor interaction on plasmid elimination by phenothiazines and imipramine in Escherichia coli.","authors":"J Molnár, Y Mándi, S Földeák","doi":"","DOIUrl":"","url":null,"abstract":"Plasmid elimination in Escherichia coli by a quaternary amine of chlorpromazine was demonstrated on different incompatibility groups of plasmid. The biological effect of the drug depends partly on the host bacteria and partly on the plasmid itself. Various receptor substrates such as adenosine, dopamine, histamine and norepinephrine do not alter the plasmid elimination by promethazine and imipramine. None of the known drug-receptors studied are involved in drug binding of the bacteria. The direct membrane action of imipramine and promethazine was demonstrated in electron microscopic studies and alterations in the bacterial membrane such as discontinuities, phase separation or rarely extensive lytic alterations were observed. Magnesium ions prevent the ultrastructural membrane alterations caused by imipramine and promethazine. There is some evidence that the drugs bind to two different receptor sites simultaneously on the plasmid replication site. The first and strongest binding has to be ionic through the side chain amino group, displacing the bivalent cations. In turn, the two aromatic rings of the fixed (ionically bound) drug molecules bind weakly through pi-electrons, hydrophobically or by a charge transfer complex. This weaker binding together with the ionic one are essential for biologic action and lead to the inhibition of plasmid replication. A schematic model of the effect of tricyclic psychotropic drugs on the bacterial membrane is proposed.","PeriodicalId":75387,"journal":{"name":"Acta microbiologica Academiae Scientiarum Hungaricae","volume":"29 1","pages":"17-25"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18093927","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Enzyme-linked immunosorbent assay in the serodiagnosis of syphilis. 酶联免疫吸附试验在梅毒血清诊断中的应用。

Acta microbiologica Academiae Scientiarum Hungaricae Pub Date : 1982-01-01

M Marschalkó, I Barna-Vetró, I Horváth

引用次数: 0