Biochimica et Biophysica Acta (BBA) - Protein Structure最新文献

{"title":"Protoheme conformations in low-spin ferrohemoproteins. Resonance raman spectroscopy","authors":"A. Desbois ,&nbsp;M. Lutz ,&nbsp;R. Banerjee","doi":"10.1016/0005-2795(81)90133-1","DOIUrl":"10.1016/0005-2795(81)90133-1","url":null,"abstract":"<div><p>The low-frequency regions of resonance Raman spectra of various low-spin ferrous forms of normal human hemoglobin, soybean leghemoglobin <em>a</em> and of horse myoglobin are reported. Differences observed among the spectra of oxygenated and nitrosyl forms of these hemoproteins show that their globins impose various low-spin heme structures. A quantitative correlation between the variable frequency of resonance Raman band II (215–271 cm⁻¹) and the iron atom-heme plane distance was observed for hemoproteins and heme models, either ferrous or ferric, high-spin or low-spin. From this correlation, the iron atom-heme plane distance should be 0.3 Å in nitrosyl and oxymyoglobin (band II at 256 cm⁻¹) whereas the iron position should be near to or in the heme plane for nitrosyl and oxy forms of hemoglobin and leghemoglobin (band II between 266 and 273 cm⁻¹). A new method is proposed for monitoring the photodissociation processes in ferrohemoproteins.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 184-192"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90133-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18213018","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":"Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding","authors":"A. Desbois ,&nbsp;M. Lutz ,&nbsp;R. Banerjee","doi":"10.1016/0005-2795(81)90132-X","DOIUrl":"10.1016/0005-2795(81)90132-X","url":null,"abstract":"<div><p>The low-frequency regions of the resonance Raman spectra of deoxygenated ferrous forms of soybean leghemoglobin <span><math><mtext>a</mtext></math></span>, horse myoglobin, sperm whale myoglobin, <em>Aplysia</em> myoglobin, stripped normal human hemoglobin (T quaternary form) and of stripped human NESdesArg-hemoglobin (R quaternary form) are reported. Differences observed among these spectra show that the globins of these hemoproteins impose various heme structures. In particular, the variable frequencies of band II (210–224 cm⁻¹) and of band I_b (121–163 cm⁻¹) show that an increase in dioxygen affinity corresponds to a decrease in Fe-N(pyrrole) bond length.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 177-183"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90132-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18213017","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 new type of Phaseolus vulgaris (cv. Pinto III) seed lectin: Isolation and characterization","authors":"Arpad Pusztai,&nbsp;George Grant,&nbsp;J.C. Stewart","doi":"10.1016/0005-2795(81)90128-8","DOIUrl":"10.1016/0005-2795(81)90128-8","url":null,"abstract":"<div><p>From the seeds of <em>Phaseolus vulgaris</em> cv. ‘Pinto III’, previously regarded as a hemagglutinin-free bean, several glycoprotein lectins were purified by conventional methods, including solubility- and salt-fractionation, continuous high-voltage free-flow electrophoresis and molecular sieve chromatography. A preparation of similar lectins was also obtained by immunoaffinity chromatography on a Sepharose-4B column to which rabbit anti-Pinto seed lectin (conventionally purified) immunoglobulins had been attached. Both preparations gave one band of 28 000–29 000 subunit weight on SDS-polyacrylamide gel electrophoresis. They were however shown to contain components, with isoelectric points in the range of pH 4.7–5.0, by isoelectric focusing on polyacrylamide gels. The relative proportion of the individual lectin components was slightly different in the two preparations. Their sedimentation coefficient, 4.34 S, was the same; however, they had a slight difference in partial specific volume values; 0.691 ml/g for the conventional and 0.700 ml/g for the affinity preparation. The average molecular weight value (<span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r,av</mtext></mn></msub><msup><mi></mi><mn>0</mn></msup></math></span>) of 52 200 for the conventional preparation was significantly lower (<span><math><mtext>P &gt; 0.1</mtext></math></span>) than the value of 55 000 for the affinity-purified lectin. The ‘Pinto III’ seed lectin molecules contained two subunits only in place of the usual four subunits of the common <em>P. vulgaris</em> lectins. There was a slight immunochemical cross-reaction between the common <em>P. vulgaris</em> and the ‘Pinto III’ seed lectins. The ‘Pinto III’ seed lectins had low haemagglutinating activity when tested with rabbit erythrocytes, while their activity was high against pronase-treated rat cells. It is suggested that the low activity against rabbit cells might be the result of the lower affinity of the dimeric lectin for the exposed sugar structures on the red cell membrane.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 146-154"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90128-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87030231","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 primary structure of the tetrahaem cytochrome c3 from Desulfovibrio desulfuricans (strain norway 4). Description of a new class of low-potential cytochrome c","authors":"Mireille Bruschi","doi":"10.1016/0005-2795(81)90137-9","DOIUrl":"https://doi.org/10.1016/0005-2795(81)90137-9","url":null,"abstract":"<div><p>The complete amino acid sequence of a tetrahaem protein, cytochrome <span><math><mtext>c</mtext><msub><mi></mi><mn>3</mn></msub></math></span> isolated from <em>Desulfovibrio desulfuricans</em> (strain Norway 4), is presented. The protein molecule consists of a single polypeptide chain of 118 residues. The sequence elucidation together with the crystallographic determination at 2.5 Å resolution which has been published provide some answers about some essential properties of this molecule. Comparison of the amino acid sequence of cytochrome <span><math><mtext>c</mtext><msub><mi></mi><mn>3</mn></msub></math></span> from <em>D. desulfuricans</em> Norway with other cytochrome <span><math><mtext>c</mtext><msub><mi></mi><mn>3</mn></msub></math></span> shows the main characteristics of the structural features of the cytochrome <span><math><mtext>c</mtext><msub><mi></mi><mn>3</mn></msub></math></span> group.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 219-226"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90137-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89995128","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":"Titles of related papers in other sections","authors":"","doi":"10.1016/0005-2795(81)90140-9","DOIUrl":"https://doi.org/10.1016/0005-2795(81)90140-9","url":null,"abstract":"","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 237-238"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90140-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136483078","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 tentative elucidation of the sequence of human triosephosphate isomerase by homology peptide mapping","authors":"Pau M. Yuan,&nbsp;John M. Talent,&nbsp;Robert W. Gracy","doi":"10.1016/0005-2795(81)90136-7","DOIUrl":"10.1016/0005-2795(81)90136-7","url":null,"abstract":"<div><p>By utilizing homologous peptide mapping and amino acid analysis of recovered peptides, it has been possible to infer much of the sequence of human triosephosphate isomerase. This has been achieved with less than 5 mg of the human enzyme. The enzyme shows a great sequence homology with the rabbit enzyme. The methods used in this study can provide a rapid procedure for gaining structural information on human enzymes available only in microgram or milligram quantities.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 211-218"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90136-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18336941","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":"Low-frequency vibrations of ferroprotoporphyrin-substituted imidazole complexes. A resonance Raman study","authors":"Alain Desbois ,&nbsp;Marc Lutz","doi":"10.1016/0005-2795(81)90131-8","DOIUrl":"10.1016/0005-2795(81)90131-8","url":null,"abstract":"<div><p>This article reports the low-frequency regions of resonance Raman spectra of five- and six-coordinated ferroprotoporphyrin complexes in aqueous solution with or without detergent. For high-spin complexes having their iron atom monocoordinated to variously substituted imidazoles or to dimethylformamide, the frequency of a band observed between 194 and 237 cm⁻¹ (labelled band II) primarily depends on the <span><math><mtext>p</mtext><mtext>K</mtext><msub><mi></mi><mn><mtext>a</mtext></mn></msub></math></span> of the axial ligand. In the absence of steric effects from the axial ligand, the lower is the <span><math><mtext>p</mtext><mtext>K</mtext><msub><mi></mi><mn><mtext>a</mtext></mn></msub></math></span> of ligand, the higher the frequency of band II. We previously assigned band II to a mode essentially involving the Fe-N(pyrrole) bonds. The above <span><math><mtext>p</mtext><mtext>K</mtext><msub><mi></mi><mn><mtext>a</mtext></mn></msub></math></span> dependence is readily explained, in the frame of this assignment, in terms of a decrease in the Fe-N(pyrrole) bond strength (and of an increase in bond length) when the basicity of the axial ligand increases. On the other hand, the alternative assignment of band II to a stretching mode of Fe-N(axial ligand) is inconsistent with the observed <span><math><mtext>p</mtext><mtext>K</mtext><msub><mi></mi><mn><mtext>a</mtext></mn></msub></math></span> dependence. As far as hexacoordinated complexes are concerned, specific bands are observed at 203, 194 and 176 cm⁻¹ for imidazole, 1-methylimidazole and pyridine, respectively. These bands are assigned, on the basis of isotopic substitutions, to a summetric stretching mode of the axial ligands [ν(N-Fe-N)]. Band II is observed at 265 cm⁻¹ for these low-spin complexes, a frequency expected from the short Fe-N(pyrrole) bond lengths of nearly planar ferroporphyrins.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 2","pages":"Pages 168-176"},"PeriodicalIF":0.0,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90131-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76324375","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":"Purification and characterization of the two forms of human plasma α2HS-glycoprotein","authors":"Fumitake Gejyo,&nbsp;Karl Schmid","doi":"10.1016/0005-2795(81)90096-9","DOIUrl":"10.1016/0005-2795(81)90096-9","url":null,"abstract":"<div><p>The two forms of <span><math><mtext>α</mtext><msub><mi></mi><mn>2</mn></msub><mtext>HS-glycoprotein</mtext></math></span> were purified from Cohn fraction VI of normal human plasma and characterized in terms of their major chemical and physicochemical properties. Separation of these two proteins was achieved by chromatography on DEAE-cellulose at pH 4.4 followed by gel filtration through Sephadex G-100. The isoelectric points of the disc gel electrophoretically and immunochemically homogeneous glycoproteins were found to be at 4.1 and 4.7 and their apparent molecular weights, as determined by SDS-polyacrylamide gel electrophoresis, were shown to be 51 000 and 56 000, respectively. The amino acid compositions of both proteins were very similar, although differences, particularly in the arginine and histidine contents, were noted. The amino- and carboxyl-terminal amino acids were found to be the same for both proteins and were threonine and alanine, and valine and leucine, respectively, suggesting that both forms of this protein consist of two polypeptide chains. The total carbohydrate moiety of the relatively basic form (14%) proved to be comparable to that of the relatively acidic form (13%). More important, however, the sialic acid content of the latter was higher than that of the former. These results suggest that the difference between the two forms of <span><math><mtext>α</mtext><msub><mi></mi><mn>2</mn></msub><mtext>HS-glycoprotein</mtext></math></span> resides both in its carbohydrate and polypeptide moieties.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 1","pages":"Pages 78-84"},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90096-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17848575","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 phosphate concentration on the kinetics of bovine liver glutamate dehydrogenase self-association","authors":"Ryoichi Tashiro,&nbsp;Akie Nishimura,&nbsp;Tohru Inoue,&nbsp;Ryosuke Shimozawa","doi":"10.1016/0005-2795(81)90087-8","DOIUrl":"10.1016/0005-2795(81)90087-8","url":null,"abstract":"<div><p>The kinetics of the self-association of bovine liver glutamate dehydrogenase was studied at various phosphate buffer concentrations (pH 7.3) at 11.5°C by means of the temperature-jump technique with scattered light detection. The observed relaxation times were well explained by the random association model of Thusius et al. With increasing phosphate concentration, the association rate constant derived from the model decreased, while the dissociation rate constant was left almost constant. Relaxation amplitude was also dependent on the phosphate concentration. The changes in the rate constant and relaxation amplitude with phosphate concentration are well elucidated by assuming that glutamate dehydrogenase is protected from association by specific masking of the association site by phosphate ions.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 1","pages":"Pages 9-15"},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90087-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18319246","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 dodecyl sulfate on the spectral properties of phenylalanyl residues in serum albumin detected by second derivative spectrophotometry","authors":"Tetsuo Ichikawa ,&nbsp;Hiroshi Terada","doi":"10.1016/0005-2795(81)90090-8","DOIUrl":"10.1016/0005-2795(81)90090-8","url":null,"abstract":"<div><p>The effect of sodium dodecyl sulfate (SDS) on the spectral properties of phenylalanine residues in bovine serum albumin was studied at neutral pH by second derivative spectrophotometry. It was found that phenylalanine residues in the interior of bovine serum albumin became almost completely exposed on the surface of the protein on formation of a so-called AD₁₂ complex. This conformational change began to be significant when 4 mol SDS bound to bovine serum albumin. At higher concentrations of SDS, when so-called AD_<em>n</em> and AD_2<em>n</em> complexes were formed, phenylalanine residues were transferred to the hydrophobic region again. This might be due to the involvement of phenylalanine residues in micelle-like clusters. Change in the conformation of bovine serum albumin involving tryptophan residues was also measured. These studies demonstrate the value of second derivative spectrophotometry in studies on conformational change of proteins.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 1","pages":"Pages 33-37"},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90090-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18320412","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}