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Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie最新文献

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The reduction of flavodoxin from Azotobacter vinelandii by pyruvate. 丙酮酸还原黄氏固氮菌黄氧还毒素的研究。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-09-01 DOI: 10.1515/znb-1972-0930
H Bothe, B Falkenberg
{"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}
引用次数: 4
Oxygen reaction of 4-hydroxybenzoate monooxygenase. 4-羟基苯甲酸单加氧酶的氧反应。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-09-01 DOI: 10.1515/znb-1972-0919
V Ullrich, F H Bernhardt, H Diehl, N Erdin, H H Ruf
{"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}
引用次数: 3
Butyryl coenzyme A dehydrogenase: studies on the specificity of the formation of acyl coenzyme A complexes with long-wavelength absorption. 丁基辅酶A脱氢酶:长波长吸收酰基辅酶A络合物形成特异性的研究。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-09-01 DOI: 10.1515/znb-1972-0926
P C Engel
{"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}
引用次数: 4
NADH dehydrogenases from Azotobacter vinelandii. 葡萄酒固氮菌NADH脱氢酶。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-09-01
D V Der Vartanian
{"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}
引用次数: 0
In vivo methylation of DNA in different organs of rat at various ages. 不同年龄大鼠不同器官DNA的体内甲基化。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-08-01 DOI: 10.1515/znb-1972-0827
D Lutz, M Löwel, H Kröger, D Kubsch, W Uecker
{"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}
引用次数: 4
[Potentiometric analysis of countercurrent net transport kinetics of K + and H + ions across the membrane of E. coli B]. [K +和H +离子在大肠杆菌B膜上逆流净输运动力学的电位分析]。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-08-01
R L'Orange, B Frommer-Evers
{"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}
引用次数: 0
Studies on esterases levels in various tissues of Uromastix Hardwickii during activity and hibernation. 活动和冬眠期间哈氏夜蛾各组织酯酶水平的研究。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-08-01 DOI: 10.1515/znb-1972-0824
F Farzana, S N Hasnain
{"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}
引用次数: 0
Differential effect of ethidium bromide and cytosine arabinoside on mitochondrial and nuclear DNA synthesis in HeLa cells. 溴化乙锭和阿拉伯糖胞嘧啶对HeLa细胞线粒体和核DNA合成的差异影响。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-08-01 DOI: 10.1515/znb-1972-0826
K Kato, K D Radsak, H Koprowski
{"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}
引用次数: 3
Acid and alkaline phosphatase levels in various tissues of a lizard during activity and hibernation. 蜥蜴活动和冬眠时各种组织中的酸性和碱性磷酸酶水平。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-08-01 DOI: 10.1515/znb-1972-0823
S Aziz, S N Hasnain, M Zain-ul-Abedin
{"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}
引用次数: 1
[Concentration and characterization of "transhydrogenase activity" and 17 -hydroxysteroid-oxidoreductase from liver cytoplasmic fraction of female rats]. [雌性大鼠肝细胞质中“转氢酶活性”和17 -羟类固醇氧化还原酶的浓度和表征]。
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie Pub Date : 1972-08-01
K Pollow, B Pollow
{"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}
引用次数: 0
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