Pyruvate is shown to be a substrate for the reduction of flavodoxin from Azotobacter vinelandii, using the phosphoroclastic enzyme system from Clostridium pasteurianum. In this reaction, the reduction of this flavoprotein proceeds beyond the semiquinone state partly to the hydroquinone form. Pyruvate is possibly the substrate for the reduction of flavodoxin in the intact organisms.
{"title":"The reduction of flavodoxin from Azotobacter vinelandii by pyruvate.","authors":"H Bothe, B Falkenberg","doi":"10.1515/znb-1972-0930","DOIUrl":"https://doi.org/10.1515/znb-1972-0930","url":null,"abstract":"Pyruvate is shown to be a substrate for the reduction of flavodoxin from Azotobacter vinelandii, using the phosphoroclastic enzyme system from Clostridium pasteurianum. In this reaction, the reduction of this flavoprotein proceeds beyond the semiquinone state partly to the hydroquinone form. Pyruvate is possibly the substrate for the reduction of flavodoxin in the intact organisms.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1090-4"},"PeriodicalIF":0.0,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0930","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15507584","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}
V Ullrich, F H Bernhardt, H Diehl, N Erdin, H H Ruf
4-hydroxybenzoate hydroxylase from Ps. putida has been studied with regard to the oxygen interaction with the reduced flavin. By rapid scanning spectrophotometry and EPR-measurements of rapidly frozen mixtures no intermediate could be established either in the presence of 4-hydroxybenzoate or the dead-end inhibitor 6-hydroxynicotinic acid.
{"title":"Oxygen reaction of 4-hydroxybenzoate monooxygenase.","authors":"V Ullrich, F H Bernhardt, H Diehl, N Erdin, H H Ruf","doi":"10.1515/znb-1972-0919","DOIUrl":"https://doi.org/10.1515/znb-1972-0919","url":null,"abstract":"4-hydroxybenzoate hydroxylase from Ps. putida has been studied with regard to the oxygen interaction with the reduced flavin. By rapid scanning spectrophotometry and EPR-measurements of rapidly frozen mixtures no intermediate could be established either in the presence of 4-hydroxybenzoate or the dead-end inhibitor 6-hydroxynicotinic acid.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1067-8"},"PeriodicalIF":0.0,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0919","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15507573","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":"Butyryl coenzyme A dehydrogenase: studies on the specificity of the formation of acyl coenzyme A complexes with long-wavelength absorption.","authors":"P C Engel","doi":"10.1515/znb-1972-0926","DOIUrl":"https://doi.org/10.1515/znb-1972-0926","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1080-1"},"PeriodicalIF":0.0,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0926","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15507580","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":"NADH dehydrogenases from Azotobacter vinelandii.","authors":"D V Der Vartanian","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1082-4"},"PeriodicalIF":0.0,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15507581","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}
We investigated in vivo labelling of DNA in single organs of female Wistar rats after application of 3H-methionine. In 40 g and 120 g rats the tritium incorporation into DNA was 10 times higher in spleen than in liver, kidney and heart. DNA methylation in newborn rats (6 — 8 g) was more pronounced in each of these organs. We demonstrated a varying degree of tritium incorporation into the different bases of DNA depending on the organs. We claim that only the values for 5-methylcytosine should be used as sole criteria of DNA methylation. Our results indi cate that DNA methylation in vivo is enhanced in those organs, where a more intensive DNA synthesis occurs.
{"title":"In vivo methylation of DNA in different organs of rat at various ages.","authors":"D Lutz, M Löwel, H Kröger, D Kubsch, W Uecker","doi":"10.1515/znb-1972-0827","DOIUrl":"https://doi.org/10.1515/znb-1972-0827","url":null,"abstract":"We investigated in vivo labelling of DNA in single organs of female Wistar rats after application of 3H-methionine. In 40 g and 120 g rats the tritium incorporation into DNA was 10 times higher in spleen than in liver, kidney and heart. DNA methylation in newborn rats (6 — 8 g) was more pronounced in each of these organs. We demonstrated a varying degree of tritium incorporation into the different bases of DNA depending on the organs. We claim that only the values for 5-methylcytosine should be used as sole criteria of DNA methylation. Our results indi cate that DNA methylation in vivo is enhanced in those organs, where a more intensive DNA synthesis occurs.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 8","pages":"992-5"},"PeriodicalIF":0.0,"publicationDate":"1972-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0827","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15511177","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":"[Potentiometric analysis of countercurrent net transport kinetics of K + and H + ions across the membrane of E. coli B].","authors":"R L'Orange, B Frommer-Evers","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 8","pages":"996-1000"},"PeriodicalIF":0.0,"publicationDate":"1972-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15511178","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}
Esterases, acetylcholinesterase and cholinesterase activities were determined in various tissues of Uromastix hardwickkii during hibernation and activity. 1. The protein concentration was significantly reduced during hibernation. 2. The esterase activity in all the tissues was found to be significantly reduced during hibernation. 3. Acetylcholinesterase activity was significantly increased in all the tissues. 4. There was no significant difference in the cholinesterase activity duriing the two periods. 5. The specific activities of all the enzymes were found to be significantly increased during hibernation.
{"title":"Studies on esterases levels in various tissues of Uromastix Hardwickii during activity and hibernation.","authors":"F Farzana, S N Hasnain","doi":"10.1515/znb-1972-0824","DOIUrl":"https://doi.org/10.1515/znb-1972-0824","url":null,"abstract":"Esterases, acetylcholinesterase and cholinesterase activities were determined in various tissues of Uromastix hardwickkii during hibernation and activity. 1. The protein concentration was significantly reduced during hibernation. 2. The esterase activity in all the tissues was found to be significantly reduced during hibernation. 3. Acetylcholinesterase activity was significantly increased in all the tissues. 4. There was no significant difference in the cholinesterase activity duriing the two periods. 5. The specific activities of all the enzymes were found to be significantly increased during hibernation.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 8","pages":"977-80"},"PeriodicalIF":0.0,"publicationDate":"1972-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0824","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15511174","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}
The effect of ethidium bromide (EB) on the synthesis of circular DNA of mammalian cells was studied by isopycnic centrifugation in a CsCl-EB solution. EB (0.1—0.5 μg/ml) interferes with the synthesis of newly-formed circular DNA of HeLa cell mitochondria and causes degradation of the pre-existing circular DNA, as well. Under the same conditions, nuclear DNA synthesis was not inhibited. This effect was not reversible at a concentration of 0.5 μg EB/ml or more. Cytosine arabinoside (ara-C) did not exhibit an effect similar to that of EB.
{"title":"Differential effect of ethidium bromide and cytosine arabinoside on mitochondrial and nuclear DNA synthesis in HeLa cells.","authors":"K Kato, K D Radsak, H Koprowski","doi":"10.1515/znb-1972-0826","DOIUrl":"https://doi.org/10.1515/znb-1972-0826","url":null,"abstract":"The effect of ethidium bromide (EB) on the synthesis of circular DNA of mammalian cells was studied by isopycnic centrifugation in a CsCl-EB solution. EB (0.1—0.5 μg/ml) interferes with the synthesis of newly-formed circular DNA of HeLa cell mitochondria and causes degradation of the pre-existing circular DNA, as well. Under the same conditions, nuclear DNA synthesis was not inhibited. This effect was not reversible at a concentration of 0.5 μg EB/ml or more. Cytosine arabinoside (ara-C) did not exhibit an effect similar to that of EB.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 8","pages":"989-91"},"PeriodicalIF":0.0,"publicationDate":"1972-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0826","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15511176","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}
1. Acid phosphatase (AcPase) and alkaline phosphatase (AlPase) activities and specific activities were determined in six different tissues of Uromastix during active and hibernating periods. 2. The protein concentration was significantly reduced in all the tissues during hibernation. 3. pH optima of acid and alkaline Pases were found to be 4.2 and 9.2 respectively. 4. AcPase activity was increased in all the tissues except liver and small intestine during hibernation. 5. AlPase activity was increased in all the tissues except small intestine during hibernation. 6. Specific activities of both the enzymes were increased during hibernation.
{"title":"Acid and alkaline phosphatase levels in various tissues of a lizard during activity and hibernation.","authors":"S Aziz, S N Hasnain, M Zain-ul-Abedin","doi":"10.1515/znb-1972-0823","DOIUrl":"https://doi.org/10.1515/znb-1972-0823","url":null,"abstract":"1. Acid phosphatase (AcPase) and alkaline phosphatase (AlPase) activities and specific activities were determined in six different tissues of Uromastix during active and hibernating periods. 2. The protein concentration was significantly reduced in all the tissues during hibernation. 3. pH optima of acid and alkaline Pases were found to be 4.2 and 9.2 respectively. 4. AcPase activity was increased in all the tissues except liver and small intestine during hibernation. 5. AlPase activity was increased in all the tissues except small intestine during hibernation. 6. Specific activities of both the enzymes were increased during hibernation.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 8","pages":"973-6"},"PeriodicalIF":0.0,"publicationDate":"1972-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0823","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15511173","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":"[Concentration and characterization of \"transhydrogenase activity\" and 17 -hydroxysteroid-oxidoreductase from liver cytoplasmic fraction of female rats].","authors":"K Pollow, B Pollow","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 8","pages":"981-8"},"PeriodicalIF":0.0,"publicationDate":"1972-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15511175","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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