{"title":"Specificity of the inhibitory effects of sugars on intestinal amino acid transfer","authors":"Janet K. Bingham, H. Newey, D.H. Smyth","doi":"10.1016/0926-6585(66)90355-4","DOIUrl":"10.1016/0926-6585(66)90355-4","url":null,"abstract":"","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 2","pages":"Pages 314-316"},"PeriodicalIF":0.0,"publicationDate":"1966-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90355-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17032595","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 occurrence of poly-β-hydroxybutyrate in the blue-green alga, Chlorogloea fritschii","authors":"N.G. Carr","doi":"10.1016/0926-6585(66)90353-0","DOIUrl":"https://doi.org/10.1016/0926-6585(66)90353-0","url":null,"abstract":"","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 2","pages":"Pages 308-310"},"PeriodicalIF":0.0,"publicationDate":"1966-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90353-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92133837","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":"Crystalline ferredoxin from the photosynthetic bacterium chromatium","authors":"Reinhard Bachofen , Daniel I. Arnon","doi":"10.1016/0926-6585(66)90345-1","DOIUrl":"10.1016/0926-6585(66)90345-1","url":null,"abstract":"<div><p>Ferredoxin has been isolated and crystallized from the photosynthetic bacterium <em>Chromatium</em>. It is similar to other ferredoxins in having an equivalent amount of iron and inorganic sulfide, a strongly electronegative oxidative-reduction potential and a capacity to substitute for native chloroplast ferredoxin in mediating the reduction of NADP<sup>+</sup>. <em>Chromatium</em> ferredoxin differs in its iron content and its more electronegative oxidation-reduction potential from the other ferredoxins that have been isolated so far.</p></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 2","pages":"Pages 259-265"},"PeriodicalIF":0.0,"publicationDate":"1966-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90345-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15487985","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":"Fluorescence and the structure of proteins VIII. Iodination of ribonuclease modified by subtilisin","authors":"Robert W. Cowgill","doi":"10.1016/0926-6585(66)90338-4","DOIUrl":"10.1016/0926-6585(66)90338-4","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Loss of fluorescence during initial stages of iodination of ribonuclease S was identical with that observed for ribonuclease A. These results indicate that ribonuclease A and ribonuclease S are very similar in general conformation and that each has a minimum of 3 and possible 4 tyrosyl residues initially susceptible to iodination. During more extensive iodination of ribonuclease S, the molecule dissociated into S-peptide and iodinated S-protein. These results suggest that extensive iodination of a protein may not be a reliable guide to the number and identity of exposed tyrosyl residues in the native molecule.</p></span></li><li><span>2.</span><span><p>2. Iodination of S-protein gave a loss of fluorescence similar to that observed for urea-denatured ribonuclease A; the results indicate that all six tyrosyl residues of S-protein are susceptible to iodination as though the structure were more open than for ribonuclease A or ribonuclease S.</p></span></li><li><span>3.</span><span><p>3. A large increase in fluorescence of partially iodinated ribonuclease A occurred during denaturation by dodecyl sulfate. This change is consistent with the proposal that non-fluorescent tyrosyl residues in the interior of the native molecule are exposed and made fluorescent during denaturation.</p></span></li></ul></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 2","pages":"Pages 189-195"},"PeriodicalIF":0.0,"publicationDate":"1966-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90338-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17032580","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":"Proton magnetic resonance study of nucleic acids","authors":"Yasuo Inoue, Koji Nakanishi","doi":"10.1016/0926-6585(66)90354-2","DOIUrl":"10.1016/0926-6585(66)90354-2","url":null,"abstract":"","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 2","pages":"Pages 311-313"},"PeriodicalIF":0.0,"publicationDate":"1966-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90354-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17032593","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":"Observations on the active transport of bile salts by rat and hamster ileum in vitro","authors":"Robert G. Faust, Shih-Min Liu Wu","doi":"10.1016/0926-6585(66)90350-5","DOIUrl":"10.1016/0926-6585(66)90350-5","url":null,"abstract":"","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 2","pages":"Pages 299-301"},"PeriodicalIF":0.0,"publicationDate":"1966-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90350-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17032589","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 (Na+K+)-activated ATPase XVII. Effect of ouabain and erythrophleine on potassium concentration and membrane potential of frog sartorius muscle","authors":"W.S. Corrie , S.L. Bonting","doi":"10.1016/0926-6585(66)90280-9","DOIUrl":"10.1016/0926-6585(66)90280-9","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The effect of ouabain and erythrophleine on K<sup>+</sup>, Na<sup>+</sup> and Cl<sup>−</sup> concentrations and membrane potential in frog sartorius muscle was studied in view of reports that changes in internal ionic concentrations would not be concerned in the effect of ouabain on membrane potential.</p></span></li><li><span>2.</span><span><p>2. The two drugs each caused a decrease in membrane potential and K<sup>+</sup> concentration. The observed change in potential agreed with the expected change calculated from the decrease in K<sup>+</sup> concentration.</p></span></li><li><span>3.</span><span><p>3. There was also an uptake of Na<sup>+</sup>, larger than the loss of K<sup>+</sup>, and an uptake of Cl<sup>−</sup> equivalent to the excess Na<sup>+</sup> uptake, as well as an uptake of water sufficient to make the entering NaCl solution isotonic.</p></span></li><li><span>4.</span><span><p>4. The results are in quantitative as well as qualitative agreement with a role of ouabain- and erythrophleine-sensitive (Na<sup>+</sup>K<sup>+</sup>)-activated ATPase in the cation transport of frog sartorius muscle.</p></span></li></ul></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 1","pages":"Pages 91-96"},"PeriodicalIF":0.0,"publicationDate":"1966-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90280-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15333463","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":"Changes in potential difference and short-circuit current produced by electrical stimulation in a nerve-skin preparation of the toad","authors":"C.S. González , J.O. Sánchez , J.B. Concha","doi":"10.1016/0926-6585(66)90297-4","DOIUrl":"10.1016/0926-6585(66)90297-4","url":null,"abstract":"","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 1","pages":"Pages 186-188"},"PeriodicalIF":0.0,"publicationDate":"1966-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90297-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17031978","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":"A re-examination of Stein's dimer theory of sugar transport in human erythrocytes","authors":"D.M. Miller","doi":"10.1016/0926-6585(66)90287-1","DOIUrl":"10.1016/0926-6585(66)90287-1","url":null,"abstract":"","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 1","pages":"Pages 156-158"},"PeriodicalIF":0.0,"publicationDate":"1966-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90287-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17033670","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":"Fluorescence of chlorophyll in photosynthetic systems II. Induction of fluorescence in isolated spinach chloroplasts","authors":"Norio Murata, Mitsuo Nishimura , Atusi Takamiya","doi":"10.1016/0926-6585(66)90273-1","DOIUrl":"10.1016/0926-6585(66)90273-1","url":null,"abstract":"<div><p>Isolated spinach chloroplasts show a simpler time course of chlorophyll fluorescence in the induction period than that reported previously with living cells. The effects on the time course of many factors (addition of photosynthetic inhibitors, Hill oxidants, heat treatment, light intensity, pre-illumination and background light) were investigated. Inhibitors such as 3(4′-chlorophenyl)-1,1-dimethylurea, and <em>o</em>-phenanthroline caused the same remarkable effect on the time course, which was different from that caused by heat treatment of the chloroplasts. The back flow of electrons, which was considered in the analysis of steady-state fluorescence in our previous paper, is also taken into consideration in the present study. A scheme is proposed to account for the findings with respect to the fluorescence during the induction period. The quantity “work integral” is introduced to correlate the observed lowering of fluorescence during the induction period with the utilization of the absorbed light energy. The concentrations of the oxidation-reduction substances in the scheme were estimated from the “work integral” obtained under varied experimental conditions.</p></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"120 1","pages":"Pages 23-33"},"PeriodicalIF":0.0,"publicationDate":"1966-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90273-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17033676","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}