Increased glycolysis in tumour tissue has first been observed by W A R B U R G in 1 9 2 3 and has since been postulated to be the origin of tumour formation 1. One possibility to increase the production of lactate, is to prevent the conversion of pyruvate, which is derived from glucose via the E m d e n M e y e r h o f pathway, into acetyl-CoA. Pyruvate will then function as a hydrogen acceptor from NADH, resulting in the formation of lactic acid. The conversion of pyruvate into acetyl-CoA is catalysed by the pyruvate dehydrogenase complex which contains covalently bound lipoic acid as cofactor 2 . This cofactor can be released by lipoamidase3 causing inactivity of the pyruvate dehydrogenase complex. Since virally induced tumours also have an increased glycolytic activity 4 , it was investigated whether tumour viruses can induce lipoamidase activity. 35S-proteins from E. coli including lipoic acid were, therefore, incubated with homogenates of yeast, known to contain lipoamidase5 . They served as a control. In addition, extracts of SV 40 — and RSV — induced tumours and homogenates of hamster kidney and chicken muscle (corresponding normal tissues) were tested. The released radioactive lipoic acid was extracted with benzene and identified by thinlayer chromatography. The radiochromatogram (see Fig. 1) shows the results obtained with the tumour induced by the DNA containing SV 40 virus. It can be seen that lipoamidase activity is present in yeast but neither in the tumour nor in the kidney tissue. The same result was obtained when a tumour induced by the R N A virus RSV was compared with chicken muscle. In both cases lipoamidase activity was absent. An increased glycolysis in virus induced tumours via an induction of lipoamidase can therefore be excluded.
{"title":"Lipoamidase activity in virus induced tumours and in the corresponding normal tissue.","authors":"H Diringer","doi":"10.1515/znb-1971-1130","DOIUrl":"https://doi.org/10.1515/znb-1971-1130","url":null,"abstract":"Increased glycolysis in tumour tissue has first been observed by W A R B U R G in 1 9 2 3 and has since been postulated to be the origin of tumour formation 1. One possibility to increase the production of lactate, is to prevent the conversion of pyruvate, which is derived from glucose via the E m d e n M e y e r h o f pathway, into acetyl-CoA. Pyruvate will then function as a hydrogen acceptor from NADH, resulting in the formation of lactic acid. The conversion of pyruvate into acetyl-CoA is catalysed by the pyruvate dehydrogenase complex which contains covalently bound lipoic acid as cofactor 2 . This cofactor can be released by lipoamidase3 causing inactivity of the pyruvate dehydrogenase complex. Since virally induced tumours also have an increased glycolytic activity 4 , it was investigated whether tumour viruses can induce lipoamidase activity. 35S-proteins from E. coli including lipoic acid were, therefore, incubated with homogenates of yeast, known to contain lipoamidase5 . They served as a control. In addition, extracts of SV 40 — and RSV — induced tumours and homogenates of hamster kidney and chicken muscle (corresponding normal tissues) were tested. The released radioactive lipoic acid was extracted with benzene and identified by thinlayer chromatography. The radiochromatogram (see Fig. 1) shows the results obtained with the tumour induced by the DNA containing SV 40 virus. It can be seen that lipoamidase activity is present in yeast but neither in the tumour nor in the kidney tissue. The same result was obtained when a tumour induced by the R N A virus RSV was compared with chicken muscle. In both cases lipoamidase activity was absent. An increased glycolysis in virus induced tumours via an induction of lipoamidase can therefore be excluded.","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"266 11","pages":"1201-2"},"PeriodicalIF":0.0,"publicationDate":"1971-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1971-1130","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15505385","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":"[Stimulation of embryonic rat cells in culture by a protein fraction isolated from fetal calf serum. I. Electrophysiological measurements on cell surface membranes].","authors":"D F Hülser, W Frank","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1045-8"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506909","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}
G Arcaya, M E Pantoja, M Pieber, C Romero, J C Tohá
The interaction of L-aromatic aminoacids with bases and nucleosides is described. Of these, ʟ-tryptophan interacts more strongly with bases and nucleosides as indicated by nuclear magnetic resonance, circular dichroism and solubility measurements. A possible ring-ring type interaction between the aminoacid and bases or nucleosides is proposed; this interaction being such that the hydrodinamic behaviour of the DNA molecule is unchanged. Ultra violet irradiated DNA is protected by ʟ-tryptophan. A mechanism of energy transfer from the DNA to tryptophan trough triplet-triplet states is discussed.
{"title":"Molecular interaction of L-tryptophan with bases, ribonucleosides and DNA.","authors":"G Arcaya, M E Pantoja, M Pieber, C Romero, J C Tohá","doi":"10.1515/znb-1971-1015","DOIUrl":"https://doi.org/10.1515/znb-1971-1015","url":null,"abstract":"The interaction of L-aromatic aminoacids with bases and nucleosides is described. Of these, ʟ-tryptophan interacts more strongly with bases and nucleosides as indicated by nuclear magnetic resonance, circular dichroism and solubility measurements. A possible ring-ring type interaction between the aminoacid and bases or nucleosides is proposed; this interaction being such that the hydrodinamic behaviour of the DNA molecule is unchanged. Ultra violet irradiated DNA is protected by ʟ-tryptophan. A mechanism of energy transfer from the DNA to tryptophan trough triplet-triplet states is discussed.","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1026-30"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1971-1015","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506906","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":"[Kinetic and chemical experiments on the decay of di-N-acetylneuraminosyl-lacto-N-tetraose by neuraminidases of myxoviruses and Vibrio cholerae].","authors":"H von Nicolai, R Drzeniek, F Zilliken","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1049-51"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506910","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":"[On a glycolipopeptide from chloroplasts and its serological properties].","authors":"D Hiedemann-van Wyk","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1052-4"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506911","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":"[Haemagglutinins in snails. A discussion of their biological function].","authors":"H Kothbauer, H Schenkel-Brunner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1082-4"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506919","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}
6,7-Dimethyl-14C-8-ribityllumazine was added to cell homogenates of Propionibacterium shermanii, previously grown anaerobically in the presence of cobaltous sulfate. This homogenates were shaken under aerobic conditions for 48 hours in order to produce vitamin B12 from the corrinoids formed during the anaerobic growth phase. The vitamin B12 was isolated and its 5,6-dimethylbenzimidazole moiety split off by acid hydrolysis. It was shown that the radioactive label of 6,7-dimethyl-14C-8-ribityllumazine was exclusively localized in the 5,6-dimethylbenzimidazole moiety of the vitamin B12 molecule. The specific radioactivity of the 5,6-dimethylbenzimidazole isolated was 18 per cent of the specific radioactivity of the 6,7-dimethyl-14C-8-ribityllumazine added. The radioactive 5,6-dimethylbenzimidazole was further degraded in order to determine the radioactivity in the different carbon atoms. It was found that 45 percent of the total radioactivity was localized in the two methyl carbons (C-10+C-11) and 47 percent in carbon atoms 4 + 7 indicating that 5,6-dimethylbenzimidazole had been formed from two molecules of 6,7-dimethyl-8-ribityllumazine.
{"title":"Biosynthesis of 5,6-dimethylbenzimidazole. Precursor-function of 6,7-dimethyl-8-ribityllumazine.","authors":"H F Kühnle, P Renz","doi":"10.1515/znb-1971-1012","DOIUrl":"https://doi.org/10.1515/znb-1971-1012","url":null,"abstract":"6,7-Dimethyl-14C-8-ribityllumazine was added to cell homogenates of Propionibacterium shermanii, previously grown anaerobically in the presence of cobaltous sulfate. This homogenates were shaken under aerobic conditions for 48 hours in order to produce vitamin B12 from the corrinoids formed during the anaerobic growth phase. The vitamin B12 was isolated and its 5,6-dimethylbenzimidazole moiety split off by acid hydrolysis. It was shown that the radioactive label of 6,7-dimethyl-14C-8-ribityllumazine was exclusively localized in the 5,6-dimethylbenzimidazole moiety of the vitamin B12 molecule. The specific radioactivity of the 5,6-dimethylbenzimidazole isolated was 18 per cent of the specific radioactivity of the 6,7-dimethyl-14C-8-ribityllumazine added. The radioactive 5,6-dimethylbenzimidazole was further degraded in order to determine the radioactivity in the different carbon atoms. It was found that 45 percent of the total radioactivity was localized in the two methyl carbons (C-10+C-11) and 47 percent in carbon atoms 4 + 7 indicating that 5,6-dimethylbenzimidazole had been formed from two molecules of 6,7-dimethyl-8-ribityllumazine.","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1017-20"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1971-1012","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506904","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}
W W Franke, D J Morré, B Deumling, R D Cheetham, J Kartenbeck, E D Jarasch, H W Zentgraf
The kinetics of synthesis and degradation of the protein constituents of nuclear membranes, endoplasmic reticulum membranes (rough-surfaced microsomes), Golgi apparatus membranes and plasma membranes were determined following a single administration of L- [guanido-14C] arginine by intraperitoneal injection. Membrane protein was determined as the fraction which resists sonication and sequential extrations with 1.5 M KCl, 0.1% deoxycholate and water to remove intravesicular, intracisternal (secretory), nucleo-, adsorbed and ribosome-associated proteins. The order of maximum labeling of membrane proteins was a) endoplasmic reticulum (nuclear membrane), b) Golgi apparatus, and c) plasma membrane. Rapid decreases in specific radioactivity followed maximal labeling of endoplasmic reticulum and Golgi apparatus membranes. These rapid turnover components of endoplasmic reticulum and Golgi apparatus were sufficient to account for labeling of plasma membranes via a flow mechanism. Incorporation of radioactivity into plasma membranes showed two distinct phases. The ultrastructural features underlying the biphasic pattern of incorporation into plasma membranes are discussed. Following initial incorporation and rapid turnover, membrane proteins were characterized by degradation kinetics approximating 1st order. Rates of degradation for Golgi apparatus and plasma membranes were faster than those for nuclear envelope and endoplasmic reticulum membranes. Assuming steady state conditions, an absolute synthetic rate of 7.1 mpg/min/avergage hepatocyte was calculated for membrane proteins of the plasma membrane. The results are compatible with intracellular movement and conversion of rough endoplasmic reticulum to plasma membrane via the membranes of the Golgi apparatus, i. e., membrane flow. Additionally, the kinetics indicate that membrane synthesis and transfer is restricted to specific parts of the endoplasmic reticulum and Golgi apparatus.
{"title":"Synthesis and turnover of membrane proteins in rat liver: an examination of the membrane flow hypothesis.","authors":"W W Franke, D J Morré, B Deumling, R D Cheetham, J Kartenbeck, E D Jarasch, H W Zentgraf","doi":"10.1515/znb-1971-1016","DOIUrl":"https://doi.org/10.1515/znb-1971-1016","url":null,"abstract":"The kinetics of synthesis and degradation of the protein constituents of nuclear membranes, endoplasmic reticulum membranes (rough-surfaced microsomes), Golgi apparatus membranes and plasma membranes were determined following a single administration of L- [guanido-14C] arginine by intraperitoneal injection. Membrane protein was determined as the fraction which resists sonication and sequential extrations with 1.5 M KCl, 0.1% deoxycholate and water to remove intravesicular, intracisternal (secretory), nucleo-, adsorbed and ribosome-associated proteins. The order of maximum labeling of membrane proteins was a) endoplasmic reticulum (nuclear membrane), b) Golgi apparatus, and c) plasma membrane. Rapid decreases in specific radioactivity followed maximal labeling of endoplasmic reticulum and Golgi apparatus membranes. These rapid turnover components of endoplasmic reticulum and Golgi apparatus were sufficient to account for labeling of plasma membranes via a flow mechanism. Incorporation of radioactivity into plasma membranes showed two distinct phases. The ultrastructural features underlying the biphasic pattern of incorporation into plasma membranes are discussed. Following initial incorporation and rapid turnover, membrane proteins were characterized by degradation kinetics approximating 1st order. Rates of degradation for Golgi apparatus and plasma membranes were faster than those for nuclear envelope and endoplasmic reticulum membranes. Assuming steady state conditions, an absolute synthetic rate of 7.1 mpg/min/avergage hepatocyte was calculated for membrane proteins of the plasma membrane. The results are compatible with intracellular movement and conversion of rough endoplasmic reticulum to plasma membrane via the membranes of the Golgi apparatus, i. e., membrane flow. Additionally, the kinetics indicate that membrane synthesis and transfer is restricted to specific parts of the endoplasmic reticulum and Golgi apparatus.","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1031-9"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1971-1016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506907","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}
Whereas ribosome preparations of freshly sliced potato disks do not show appreciable activity in an in-vitro amino acid incorporation system, aging of the tissue leads to a greatly enhanced incorporation activity which reaches its maximum 24 hours after slicing. If ribosomes from freshly excised disks are provided with polyuridylic acid, their activity in the incorporation of phenylalanine is increased about 8 fold. Moreover, an RNA-fraction can be dissociated by EDTA from ribosomes of aged potato tuber slices, which sediments at 15 —18S, has a base composition different from that of 16S — rRNA, 5S-and 4S —RNA, and is not present on ribosomes of fresh slices. Its appearance is inhibited by actinomycin D and therefore most probably dependent on transcription. This compound, purified from sucrose gradients, enhances in vitro leucine incorporation into peptide material by ribosomes of fresh potato slices. The possibility is discussed that this fraction-among other factors-is responsible for the enhanced protein synthesis after slicing plant storage organs, and is indicative of a general derepression phenomenon in these tissues.
{"title":"Activation of protein synthesis in aging potato tuber slices.","authors":"G Kahl","doi":"10.1515/znb-1971-1023","DOIUrl":"https://doi.org/10.1515/znb-1971-1023","url":null,"abstract":"Whereas ribosome preparations of freshly sliced potato disks do not show appreciable activity in an in-vitro amino acid incorporation system, aging of the tissue leads to a greatly enhanced incorporation activity which reaches its maximum 24 hours after slicing. If ribosomes from freshly excised disks are provided with polyuridylic acid, their activity in the incorporation of phenylalanine is increased about 8 fold. Moreover, an RNA-fraction can be dissociated by EDTA from ribosomes of aged potato tuber slices, which sediments at 15 —18S, has a base composition different from that of 16S — rRNA, 5S-and 4S —RNA, and is not present on ribosomes of fresh slices. Its appearance is inhibited by actinomycin D and therefore most probably dependent on transcription. This compound, purified from sucrose gradients, enhances in vitro leucine incorporation into peptide material by ribosomes of fresh potato slices. The possibility is discussed that this fraction-among other factors-is responsible for the enhanced protein synthesis after slicing plant storage organs, and is indicative of a general derepression phenomenon in these tissues.","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1064-7"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1971-1023","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506913","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":"[Ethylation of guanine-N-7 in the nucleic acids of rat embryos and liver by ethylnitrosourea].","authors":"R Goth, M F Rajewsky","doi":"10.1515/znb-1971-1032","DOIUrl":"https://doi.org/10.1515/znb-1971-1032","url":null,"abstract":"","PeriodicalId":23706,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete","volume":"26 10","pages":"1076-7"},"PeriodicalIF":0.0,"publicationDate":"1971-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1971-1032","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15506915","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}