Arne Jensen, Olav Aasmundrud , Kjell E. Eimhjellen
{"title":"Chlorophylls of photosynthetic bacteria","authors":"Arne Jensen, Olav Aasmundrud , Kjell E. Eimhjellen","doi":"10.1016/0926-6577(64)90089-0","DOIUrl":"10.1016/0926-6577(64)90089-0","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The chlorophylls and the corresponding phaeophytins of 18 species of photosynthetic bacteria have been characterized by paper chromatography and by absorption spectra in visible light.</p></span></li><li><span>2.</span><span><p>2. Except for one species of Rhodopseudomonas which contained bacteriochlorophyll <em>b</em>, all the Thiorhodaceae (four) and the Athiorhodaceae (nine) species investigated as well as <em>Rhodomicrobium vannielii</em> had bacteriochlorophyll <em>a</em> as the only detectable chlorophyll.</p></span></li><li><span>3.</span><span><p>3. The chlorophyll-770 of Chlorobacteriaceae (four strains or species) was found to be spectroscopically and chromatographically identical with bacteriochlorophyll <em>a</em>.</p></span></li><li><span>4.</span><span><p>4. The chlorobium chlorophylls-650 and -660 were each separated by paper chromatography into three fractions. In the case of chlorobium chlorophyll-650 two of the fractions each gave rise to one phaeophytin, whereas the last fraction gave three phaeophytins. All phaeophytins had identical absorption spectra, but exhibited different <em>R</em><sub><em>F</em></sub>-values on paper chromatograms.</p></span></li><li><span>5.</span><span><p>5. In addition to the chlorophylls mentioned above, all the species of the Chlorobacteriaceae contained trace amounts of a hitherto undescribed chlorophyllous pigment.</p></span></li><li><span>6.</span><span><p>6. A revision of the current nomenclature for bacterial chlorophyll is proposed.</p></span></li></ul></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90089-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23800716","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":"Studies on the surface and cytoplasmic membranes of Ehrlich ascites carcinoma cells","authors":"Donald F. Hoelzl Wallach, Donna Ullrey","doi":"10.1016/0926-6577(64)90104-4","DOIUrl":"10.1016/0926-6577(64)90104-4","url":null,"abstract":"<div><p>A membrane fraction isolated from Ehrlich ascites carcinoma microsomes contians an ATP phosphohydrolas which is strongly stimulated by K<sup>+</sup> in the presence of Na<sup>+</sup>. The enzyme system has an absolute requirement for Na<sup>+</sup> and Mg<sup>2+</sup>, but a number of monovalent cations can simulate K<sup>+</sup>. Ca<sup>2+</sup>, ADP and ouabain are inhibitory. The enzyme is believed to be associated with plasma membrane fragments.</p><p>The quantitative relationships between enzyme activity and reactant concentration is presented and the probable relationship between ion transport in the whole cell and the alkali-cation-sensitive ATP phosphohydrolase is discussed.</p></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90104-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23802391","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":"Oxidation-reduction changes of cytochromes in lobster heart","authors":"José Ramírez","doi":"10.1016/0926-6577(64)90108-1","DOIUrl":"10.1016/0926-6577(64)90108-1","url":null,"abstract":"","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90108-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78147080","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":"Effect of electric field on F-actin oriented by flow","authors":"Shoyu Kobayashi","doi":"10.1016/0926-6577(64)90097-X","DOIUrl":"10.1016/0926-6577(64)90097-X","url":null,"abstract":"<div><p>Pulsed electric fields were applied to F-actin oriented by flow and the process of dis- orientation was followed by birefringence measurements. An electric field parallel to the filament axis of F-actin produced a large disorientation effect whereas a perpendicular field produced a small effect. The analysis of the birefringence decrease in normal and reversed pulses at various field strengths suggests that F-actin has a large permanent dipole moment perpendicular to the filament axis. The marked disorientation effect of the parallel field on F-actin vanished on addition of H-meromyosin. On dissociation of the complex of F-actin and H-meromyosin by the addition of ATP the disorientation effect of the parallel field was again observed. This result suggests that a strong electric interaction exists between (permanent) dipoles of F-actin and H-meromyosin.</p></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90097-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77534719","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":"Photoreduction of nicotinamide-adenine dinucleotide by a cell-free system from Chromatium","authors":"S.L. Hood","doi":"10.1016/0926-6577(64)90088-9","DOIUrl":"10.1016/0926-6577(64)90088-9","url":null,"abstract":"<div><p>A small particle fraction has been prepared from <em>Chromatium</em> which reduces NAD by both photo and dark reactions. The reductions are stimulated by the addition of two <em>Chromatium</em> enzymes, a flavoprotein and cyrstalline ferredoxin.</p></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90088-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23800715","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":"Evidence of bacteriochlorophyll dimerization in the chlorophyll-protein complex from green photosynthetic bacteria","authors":"John M. Olson","doi":"10.1016/0926-6577(64)90113-5","DOIUrl":"10.1016/0926-6577(64)90113-5","url":null,"abstract":"","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90113-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23802398","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":"Inhibition of greening of heat-bleached Euglena by streptomycin","authors":"John L. Mego","doi":"10.1016/0926-6577(64)90114-7","DOIUrl":"10.1016/0926-6577(64)90114-7","url":null,"abstract":"","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90114-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23802399","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":"Influence of cysteine on the photochemical decomposition of thymidyl-(5′-3′)-bromodeoxyuridine","authors":"A. Haug","doi":"10.1016/0926-6577(64)90090-7","DOIUrl":"10.1016/0926-6577(64)90090-7","url":null,"abstract":"<div><p>Irradiating a solution of thymidyl-(5′-3′)-bromodeoxyuridine with monochromatic, ultraviolet light yields one main photo-product, an intramolecular dimer, containing no Br and a cyclobutene ring structure. In the presence of cysteine and ultraviolet radiation the dimer is further decomposed to a photo-product characterized by an end-absorption spectrum. This compound contains one S atom per dinucleotide and cannot be reverted by irradiation at 2400 Å. The quantum yields of this sulfhydryl addition are measured as a function of wavelength. The reaction kinetics and the biological implication of this process, which is possibly radio-protective, are discussed.</p></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90090-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87755988","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":"Volume changes in isolated myofibrils","authors":"R.J. Baskin","doi":"10.1016/0926-6577(64)90095-6","DOIUrl":"10.1016/0926-6577(64)90095-6","url":null,"abstract":"<div><p>Volume changes in glycerol-extracted myofibrils were studied. The effect of pH, ion content and ATP concentration on the change in volume was determined. A volume change greater than that attributed to ATP dephosphorylation was observed. The magnitude of the volume change of the entire system was 10<sup>−3</sup> cm<sup>3</sup> whereas that due to dephosphorylation was 10<sup>−6</sup> cm<sup>3</sup>. The ratio of ATPase activity in a volume decrease to that in a volume increase was found to be approx. 10:1. The total amount of volume decrease measured approx. 0.028 cm<sup>3</sup>/g of muscle with a fresh myo fibril preparation. The volume increase which was observed upon the addition of large amounts of ATP amounted to approx. 0.036 cm<sup>3</sup>/g of muscle. The relationship between the volume changes and molecular reorganization of the myofibril proteins was discussed. It was concluded that either a large configurational change occurs in the myofibril proteins during an ATP-induced contraction or relaxation, or that the volume changes are related to the dissociation and association of actin and myosin filaments</p></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90095-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23802382","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}