{"title":"Interactions with the immune system","authors":"V. Lévy-Frébault","doi":"10.1016/0769-2609(88)90089-0","DOIUrl":"10.1016/0769-2609(88)90089-0","url":null,"abstract":"","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Page 737"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90089-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"102716583","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}
{"title":"Absence of Listeria species in lower animals","authors":"H.E Müller","doi":"10.1016/0769-2609(88)90077-4","DOIUrl":"10.1016/0769-2609(88)90077-4","url":null,"abstract":"<div><p>La présence de <em>Listeria</em> a été évaluée chez animaux inférieurs, qui ont été collectionnés à partir de deux territoires agricoles: 1) une région sans fumiers ni irrigation par des eaux d égouts; 2) une région irriguée par des eaux d'égouts avec environ 10<sup>3</sup>–10<sup>4</sup><em>Listeria</em>/l. Aucune espèce de <em>Listeria</em> n'a été isolée bien que quelques publications aient décrit la présence de <em>Listeria</em> chez des animaux inférieurs aquatiques et chez des insectes hématophages. Cette étude suggère que les animaux inférieurs ne sont que des vecteurs passifs et non les hôtes naturels de <em>Listeria</em>.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Pages 727-730"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90077-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14379611","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}
{"title":"Zonal turnover of cell poles of Bacillus subtilis","authors":"G Kirchner , M.A Kemper , A.L Koch , R.J Doyle","doi":"10.1016/0769-2609(88)90069-5","DOIUrl":"10.1016/0769-2609(88)90069-5","url":null,"abstract":"<div><p>Turnover of cell walls of <em>Bacillus subtilis</em> occurs in three distinct phases: a lag phase, a relatively rapid phase persisting for 2–3 generations and a much slower phase continuing for several additional generations. A lectin probe revealed that cell pole material was lost during the slow phase of turnover and that the loss of wall occurred in zones, beginning at the cylinder-pole junction and continuing to the cell tip. This is in contrast to cell wall turnover in cylinders where turnover occurs randomly at many surface sites.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Pages 645-654"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90069-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14282364","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}
{"title":"Mutagnenéses et protéines","authors":"","doi":"10.1016/0769-2609(88)90083-X","DOIUrl":"https://doi.org/10.1016/0769-2609(88)90083-X","url":null,"abstract":"","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Page 733"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90083-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136402713","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}
R. Janati-Idrissi, A.M. Junelles, H. Petitdemange, R. Gay
{"title":"Regulation of coenzyme a transferase and acetoacetate decarboxylase activities in clostridium acetobutylicum","authors":"R. Janati-Idrissi, A.M. Junelles, H. Petitdemange, R. Gay","doi":"10.1016/0769-2609(88)90073-7","DOIUrl":"10.1016/0769-2609(88)90073-7","url":null,"abstract":"<div><p>The activity of two enzymes involved in acetone production in <em>Clostridium acetobutylicum</em>, acetoacetate decarboxylase and coenzyme A transferase, was studied under acidogenic or solventogenic conditions. Acetoacetate decarboxylase activity was low under acidogenic conditions and after pyruvate addition. Under the same conditions, coenzyme A transferase activity was high. A mutant which lacked acetoacetate decarboxylase activity but was positive for coenzyme A transferase activity was isolated.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Pages 683-688"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90073-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14381210","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}
{"title":"Comité OMS d'experts de la Standardisation biologique","authors":"","doi":"10.1016/0769-2609(88)90087-7","DOIUrl":"https://doi.org/10.1016/0769-2609(88)90087-7","url":null,"abstract":"","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Page 736"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90087-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136403097","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}
{"title":"Assay for detection of adenosine phosphorylase from mycoplasmas","authors":"C Bonissol , T Sasaki , B Stoiljkovic","doi":"10.1016/0769-2609(88)90075-0","DOIUrl":"10.1016/0769-2609(88)90075-0","url":null,"abstract":"<div><p>A microtechnique is described which permits simple evaluation of the activity of the enzyme adenosine phoshorylase (AdoP), present in all mycoplasmas tested thus far. The good solubility and stability of AdoP and the sensitivity of the assay should be advantageous in detecting mycoplasmas in biological samples such as animal sera, cell cultures and vaccines.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Pages 703-715"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90075-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14281055","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}
{"title":"Chitosan as flocculant for concentrating Euglena gracilis cultures","authors":"P Gualtieri, L Barsanti, V Passarelli","doi":"10.1016/0769-2609(88)90076-2","DOIUrl":"10.1016/0769-2609(88)90076-2","url":null,"abstract":"<div><p>The practical criteria for the usefulness of an algal separation process for laboratory routine being effectiveness and time consumption, we tested the feasibility of a flocculation procedure to harvest large volumes of <em>Euglena gracilis</em> in culture. This procedure turned out to be a technically viable system which avoided tedious centrifugation and preserved <em>E. gracilis</em> flagellar apparatus integrity.</p><p><em>E. gracilis</em> cultures were treated with chitosan, a by-product derived from chitin from the exoskeleton of crustaceans. Since this polymer carries a positive charge, it functions as a polycationic coagulating agent by adsorbing onto particles in suspension and by bridging together into agglomerates, or flocs. A 96–98% reduction of suspended cells in cultures with 200 mg/l of chitosan, at pH 7.5, was obtained.</p></div>","PeriodicalId":77666,"journal":{"name":"Annales de l'Institut Pasteur. Microbiology","volume":"139 6","pages":"Pages 717-726"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0769-2609(88)90076-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14281058","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}
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