{"title":"Acetohydroxyacid Synthase from Cell Suspension Cultures of Isatis tinctoria l. and Ruta graveolens l.","authors":"Walter Maier , Brigitte Schumann , Detlef Gröger","doi":"10.1016/S0015-3796(11)80003-X","DOIUrl":"10.1016/S0015-3796(11)80003-X","url":null,"abstract":"<div><p>Acetohydroxyacid synthase (EC 4.1.3.18) has been extracted from cell suspension cultures of <em>Isatis tinctoria</em> (Cruciferae) and <em>Ruta graveolens</em> (Rutaceae). A combination of salt precipitation, gel filtration and ion exchange chromatography was used for partial purification. The apparent molecular masses of AHAS were M<sub>r</sub> 82,000 and 85,000 for <em>Isatis</em> and <em>Ruta</em>, respectively. FAD was an absolute requirement for AHAS activity. The apparent K<sub>m</sub> values of <em>Isatis</em>-AHAS are the following ones: FAD 6,3 × 10<sup>−6</sup> M; TPP 6,3 × 10<sup>−6</sup> M; pyruvate 7 × 10<sup>−3</sup>, and 6 × 10<sup>−3</sup> M (for <em>Ruta</em>-AHAS).</p><p>Branched-chain amino acids and chlorsulfuron are feedback inhibitors for <em>Isatis</em>-AHAS but acetohydroxyacid synthase from <em>Ruta</em> is not sensitive to valine, leucine and isoleucine.</p></div>","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 3","pages":"Pages 161-167"},"PeriodicalIF":0.0,"publicationDate":"1992-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80003-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83674058","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":"Pressemitteilung","authors":"","doi":"10.1016/S0015-3796(11)80012-0","DOIUrl":"https://doi.org/10.1016/S0015-3796(11)80012-0","url":null,"abstract":"","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 3","pages":"Page 207"},"PeriodicalIF":0.0,"publicationDate":"1992-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80012-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137191034","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":"","authors":"J. Hofemeister","doi":"10.1016/S0015-3796(11)80010-7","DOIUrl":"10.1016/S0015-3796(11)80010-7","url":null,"abstract":"","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 3","pages":"Page 205"},"PeriodicalIF":0.0,"publicationDate":"1992-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80010-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73401948","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":"","authors":"J. Matschke","doi":"10.1016/S0015-3796(11)80008-9","DOIUrl":"https://doi.org/10.1016/S0015-3796(11)80008-9","url":null,"abstract":"","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 3","pages":"Pages 202-203"},"PeriodicalIF":0.0,"publicationDate":"1992-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80008-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137019732","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":"","authors":"W. Bergmann","doi":"10.1016/S0015-3796(11)80021-1","DOIUrl":"10.1016/S0015-3796(11)80021-1","url":null,"abstract":"","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 2","pages":"Page 135"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80021-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81216657","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}
Wolfgang Dreier , Erhard Preusser , Marianne Gründel
{"title":"The Regulation of the Activity of Soluble Starch Synthase in Spinach Leaves by a Calcium-Calmodulin Dependent Protein Kinase","authors":"Wolfgang Dreier , Erhard Preusser , Marianne Gründel","doi":"10.1016/S0015-3796(11)80013-2","DOIUrl":"10.1016/S0015-3796(11)80013-2","url":null,"abstract":"<div><p>Soluble starch synthase from spinach leaves can use ADPG and UDPG for chain elongation in the presence of an appropriate primer (glycogen, amylopectin). Whereas calcium ions alone or in combination with calmodulin (CaM) insignificantly reduce the biosynthesis of starch, ATP causes a substantial decrease in activity. EDTA and ADP on the other hand promote the incorporation of glucose. Using CaM-Sepharose-4B, a protein kinase (molecular weight 68 kD) could be isolated. This protein kinase is able to eliminate the ATP-induced inhibition in a calcium-CaM dependent way in the presence of Mg<sup>++</sup>. The enhancement of the starch synthase activity by the protein kinase is Ca<sup>++</sup> and CaM specific. The optimum is observed at 5 mM ca<sup>++</sup> and 1.45 · 10<sup>-7</sup> mM CaM. The Ca-CaM dependence of protein kinase was proven by CaM antagonists (fluphenazine, trifluoperazine and calmidazolium at 5 · w<sup>-5</sup> M). Fluoride on the other hand enhanced the starch synthesis via the inhibition of a protein phosphatase. The phosphorylation of starch synthase was demonstrated by the incorporation of <sup>32</sup>P after application of <sup>32</sup>P-γ-ATP in the presence of the protein kinase.</p></div>","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 2","pages":"Pages 81-96"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80013-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82655078","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":"H2O2 Metabolism During Senescence of Two Submerged Angiosperms Hydrilla and Ottelia: Changes in Enzyme Activities in Light and Darkness","authors":"Hasna Hena Begam, M.A. Choudhuri","doi":"10.1016/S0015-3796(11)80017-X","DOIUrl":"10.1016/S0015-3796(11)80017-X","url":null,"abstract":"<div><p>Study of the role of H<sub>2</sub>O<sub>2</sub> on senescence and photobleaching of chlorophyll revealed that pretreatment with H<sub>2</sub>O<sub>2</sub> enhanced the loss of chlorophyll and protein in <em>Hydrilla verticillata</em> (L.f.) Royle and <em>Ottelia alismoides</em> (L.) Pers. leaves, more markedly so in the light than in the dark. Endogenous H<sub>2</sub>O<sub>2</sub> and free phenol contents significantly increased during senescence, the effect being larger in light than in darkness. DCP (2,4-dichlorophenol, a monophenol) greatly accelerated the loss of chlorophyll and protein in the light while catechol (a diphenol) significantly retarded them. However, both these phenols retarded the loss of these components in the dark. Both peroxidase and chlorophyll oxidase activity greatly increased in light over dark treatment. The activity of superoxide dismutase and catalase declined more markedly in light than in darkness in either species. The possible involvement of oxygen free radicals and light-induced phenol peroxidase - H<sub>2</sub>O<sub>2</sub> system in the photobleaching of chlorophyll and senescence development in the two submerged angiosperms has been suggested.</p></div>","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 2","pages":"Pages 105-115"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80017-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74946043","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":"Characterization of a Suspension Culture of Chelidonium majus L. on Growth and Accumulation of Sanguinarine","authors":"Franca Tomè , Maria Laura Colombo","doi":"10.1016/S0015-3796(11)80018-1","DOIUrl":"10.1016/S0015-3796(11)80018-1","url":null,"abstract":"<div><p>Cell suspension cultures of <em>C. majus</em> L. — obtained from callus — were characterized on growth and on accumulation of isoquinoline alkaloids. The liquid batch cultures consisted of coarse cell aggregates; their fresh volume becames triple each 14 days after subcultures. Cell cultures were found to produce relatively large amounts of isoquinoline alkaloids; sanguinarine is accumulated as main alkaloid and also released into the medium.</p></div>","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 2","pages":"Pages 116-120"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80018-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86036828","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":"Partial Purification of Toxin from Curvularia lunata (Wakker) Boedijn","authors":"H.N. Gour , P.D. Nitharwal , Sanjeev Agarwal","doi":"10.1016/S0015-3796(11)80020-X","DOIUrl":"10.1016/S0015-3796(11)80020-X","url":null,"abstract":"<div><p>The fungus isolated from diseased tissues of pearl millet leaves was identified as <em>Curvularia lunata</em>. A toxin, isolated from 14 day old culture filtrate of <em>C. lunata</em>, was partially purified by ammonium sulfate fractionation followed by gel filtration through Sephadex G-100. The toxin was heat stable and soluble in water and acetate buffer at <em>p</em>H 5.5 to 6.0. Toxin was found to be most active at <em>p</em>H 5.5. The partially purified toxin showed some degree of host specificity. Different host varieties were screened for disease resistance. Toxin also affected cell permeability of susceptible host tissues.</p></div>","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 2","pages":"Pages 128-135"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80020-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80655575","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":"Pressemitteilung","authors":"","doi":"10.1016/S0015-3796(11)80016-8","DOIUrl":"https://doi.org/10.1016/S0015-3796(11)80016-8","url":null,"abstract":"","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 2","pages":"Page 104"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80016-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136573043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}