The isoelectric behaviour of the NDV-induced rabbit serum interferon was compared with different NDV-induced interferons from rabbit cells. The activity of serum interferon was found in a pH range from 4.6—6.2. In contrast, the isoelectric positions of cell interferons could be demonstrated in a more acid pH range between pH 3.7 and 5.0.
{"title":"Isoelectric behaviour of different rabbit interferons induced by Newcastle disease virus.","authors":"W Hellmann, H Kohlhage","doi":"10.1515/znb-1972-1126","DOIUrl":"https://doi.org/10.1515/znb-1972-1126","url":null,"abstract":"The isoelectric behaviour of the NDV-induced rabbit serum interferon was compared with different NDV-induced interferons from rabbit cells. The activity of serum interferon was found in a pH range from 4.6—6.2. In contrast, the isoelectric positions of cell interferons could be demonstrated in a more acid pH range between pH 3.7 and 5.0.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 11","pages":"1411-4"},"PeriodicalIF":0.0,"publicationDate":"1972-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15512315","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 reactions of ᴅ-amino acid oxidase with β-chloro-ᴅ-alanine and β-chloro-ʟ-alanine have been described. Both the holoenzyme and the apoenzyme catalyse the deamination of β-chloro-ʟ-alanine to keto acid without any consumption of oxygen or oxidation-reduction of the enzyme-bound FAD. The anaerobic reaction of the holoenzyme with β-chloro-ᴅ-alanine involves three phases with respect to the reduction of the enzyme-bound FAD, the rapid formation of an intermediate spectral species followed by a steady state of this intermediate and the last decay of the intermediate to the fully reduced enzyme. The rate of keto acid formation decreases as the reaction proceeds and ceases at the beginning of the conversion of the intermediate to the fully reduced enzyme. The aerobic reaction of the holoenzyme with β-chloro-ᴅ-alanine is biphasic. The first rapid oxygen consumption is followed by the second slow oxygen consumption. The second slow phase disappears by treating the enzyme with glutathione before the addition of substrate.
{"title":"On the reaction of D-amino acid oxidase with -chloroalanine.","authors":"Y Miyake, T Abe, T Yamano","doi":"10.1515/znb-1972-1118","DOIUrl":"https://doi.org/10.1515/znb-1972-1118","url":null,"abstract":"The reactions of ᴅ-amino acid oxidase with β-chloro-ᴅ-alanine and β-chloro-ʟ-alanine have been described. Both the holoenzyme and the apoenzyme catalyse the deamination of β-chloro-ʟ-alanine to keto acid without any consumption of oxygen or oxidation-reduction of the enzyme-bound FAD. The anaerobic reaction of the holoenzyme with β-chloro-ᴅ-alanine involves three phases with respect to the reduction of the enzyme-bound FAD, the rapid formation of an intermediate spectral species followed by a steady state of this intermediate and the last decay of the intermediate to the fully reduced enzyme. The rate of keto acid formation decreases as the reaction proceeds and ceases at the beginning of the conversion of the intermediate to the fully reduced enzyme. The aerobic reaction of the holoenzyme with β-chloro-ᴅ-alanine is biphasic. The first rapid oxygen consumption is followed by the second slow oxygen consumption. The second slow phase disappears by treating the enzyme with glutathione before the addition of substrate.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 11","pages":"1376-8"},"PeriodicalIF":0.0,"publicationDate":"1972-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-1118","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15512309","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}
F Koenig, W Menke, H Craubner, G H Schmid, A Radunz
After solubilization of stroma-freed chloroplasts with deoxycholate, the lipids and the detergent used are separated from the proteins by gel filtration. In this way not denatured pigment-con-taining protein preparations were obtained. The particles in fraction 1 exhibited a molecular weight of 600 000 and contained an average of 25 chlorophyll molecules. The circular dichroism spectrum showed exciton splitting of the red band. The particles in fraction 2 contained 1 chlorophyll molecule and exhibited a molecular weight of 110 000. The particles in fraction 3 also contained only 1 chlorophyll molecule and had a molecular weight of between 80 000 and 100 000. Pure preparations of fraction 1 only carried out the methylviologen Mehler reaction with the dichlorophenol indophenol/ascorbate couple as electron donor. Fraction 3 only reduced ferricyanide with diphenylcarbazide as an electron donor in the light. Fraction 2 exhibited both the photosystem I reaction and the photosystem II reaction. An antiserum to extracted fraction 1 does not inhibit electron transport in the intact lamellar system. The photoreduction of methylviologen is only inhibited after disruption of the thylakoids. The antiserum to fraction 2 inhibits the photoreduction of methylviologen in the intact lamellar system. Consequently, one inhibition site for this photosystem I reaction must be located on the inner and another on the outer surface of the thylakoid membrane. In addition, antibodies to fraction 1 are specifically adsorbed onto the lamellar system without any effect on electron transport and without a concomitant agglutination. Antibodies to fraction 3 partially inhibit the photoreduction of ferricyanide with diphenylcarbazide as an electron donor in the intact lamellar system. Hence, the inhibition site of this system II reaction is located on the outer surface of the thylakoids. We have reason to believe that the inhibition sites not reacting are located in the partitions, which are not accessible to antibodies.
{"title":"Photochemically active chlorophyll-containing proteins from chloroplasts and their localization in the thylakoid membrane.","authors":"F Koenig, W Menke, H Craubner, G H Schmid, A Radunz","doi":"10.1515/znb-1972-1023","DOIUrl":"https://doi.org/10.1515/znb-1972-1023","url":null,"abstract":"After solubilization of stroma-freed chloroplasts with deoxycholate, the lipids and the detergent used are separated from the proteins by gel filtration. In this way not denatured pigment-con-taining protein preparations were obtained. The particles in fraction 1 exhibited a molecular weight of 600 000 and contained an average of 25 chlorophyll molecules. The circular dichroism spectrum showed exciton splitting of the red band. The particles in fraction 2 contained 1 chlorophyll molecule and exhibited a molecular weight of 110 000. The particles in fraction 3 also contained only 1 chlorophyll molecule and had a molecular weight of between 80 000 and 100 000. Pure preparations of fraction 1 only carried out the methylviologen Mehler reaction with the dichlorophenol indophenol/ascorbate couple as electron donor. Fraction 3 only reduced ferricyanide with diphenylcarbazide as an electron donor in the light. Fraction 2 exhibited both the photosystem I reaction and the photosystem II reaction. An antiserum to extracted fraction 1 does not inhibit electron transport in the intact lamellar system. The photoreduction of methylviologen is only inhibited after disruption of the thylakoids. The antiserum to fraction 2 inhibits the photoreduction of methylviologen in the intact lamellar system. Consequently, one inhibition site for this photosystem I reaction must be located on the inner and another on the outer surface of the thylakoid membrane. In addition, antibodies to fraction 1 are specifically adsorbed onto the lamellar system without any effect on electron transport and without a concomitant agglutination. Antibodies to fraction 3 partially inhibit the photoreduction of ferricyanide with diphenylcarbazide as an electron donor in the intact lamellar system. Hence, the inhibition site of this system II reaction is located on the outer surface of the thylakoids. We have reason to believe that the inhibition sites not reacting are located in the partitions, which are not accessible to antibodies.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 10","pages":"1225-38"},"PeriodicalIF":0.0,"publicationDate":"1972-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-1023","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15508349","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":"[The modification of wing patterns in the peacock butterfly Inachis io L. (nymphalidae, Lepidoptera) by physical means and their radioactive labelling].","authors":"R Hamm, M Lüdicke","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 10","pages":"1258-63"},"PeriodicalIF":0.0,"publicationDate":"1972-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15508352","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}
Alkaryl triazenes were synthesized in two steps from the isolated intermediary diazonium tetrafluoroborates and hexafluorophosphates by coupling the arenediazonium cations with dimethylamine in an aqueous solution but without the use of mineral base. The method enables the preparation of triazenes which are not readily accessible by conventional procedures; it also leads to higher yields and purer products in the preparation of known compounds.
{"title":"Synthesis of biologically active triazenes from isolable diazoniums salts.","authors":"G F Kolar","doi":"10.1515/znb-1972-1016","DOIUrl":"https://doi.org/10.1515/znb-1972-1016","url":null,"abstract":"Alkaryl triazenes were synthesized in two steps from the isolated intermediary diazonium tetrafluoroborates and hexafluorophosphates by coupling the arenediazonium cations with dimethylamine in an aqueous solution but without the use of mineral base. The method enables the preparation of triazenes which are not readily accessible by conventional procedures; it also leads to higher yields and purer products in the preparation of known compounds.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 10","pages":"1183-5"},"PeriodicalIF":0.0,"publicationDate":"1972-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-1016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15508342","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":"Demonstration of blood group substance H and galactosyl groups on Candida albicans.","authors":"W P Herrmann, G Uhlenbruck","doi":"10.1515/znb-1972-1037","DOIUrl":"https://doi.org/10.1515/znb-1972-1037","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 10","pages":"1284-5"},"PeriodicalIF":0.0,"publicationDate":"1972-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-1037","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15512625","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":"[The reduction of the B 12 -vitamins by carbon monoxide].","authors":"M Moskophidis, W Friedrich, C M Pohl","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 10","pages":"1175-82"},"PeriodicalIF":0.0,"publicationDate":"1972-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15508341","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":"Cleavage of ATP by mouse uterine chromatin after in vivo administration of oestradiol.","authors":"H R Maurer","doi":"10.1515/znb-1972-1028","DOIUrl":"https://doi.org/10.1515/znb-1972-1028","url":null,"abstract":"","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 10","pages":"1267-70"},"PeriodicalIF":0.0,"publicationDate":"1972-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-1028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15512624","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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