Biochimica et Biophysica Acta (BBA) - Protein Structure最新文献_第9页

Conformational changes of the subunits Clq, Clr and Cls of human complement component Cl demonstrated by 125I labeling 125I标记显示人补体成分Cl的亚基Clq、Clr和Cls构象变化

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90057-X

Johann Bauer, Guenter Valet

{"title":"Conformational changes of the subunits Clq, Clr and Cls of human complement component Cl demonstrated by 125I labeling","authors":"Johann Bauer, Guenter Valet","doi":"10.1016/0005-2795(81)90057-X","DOIUrl":"10.1016/0005-2795(81)90057-X","url":null,"abstract":"<div>C1s and C1r proenzymes and enzymes (C1s, C1r) and C1q were labeled with 125I. The distribution of the 125I label between H- and L-chain of C1s was only slightly dependent on the state of activation of C1s, and approx. 90% of the label was found in the H-chain. In the Clr proenzyme molecules 50% of the label was incorporated into the H-chain. The C1r H-chain label was reduced to 10% on activation of C1r to C1r, while the L-chain label increased to 90% of the total label. The presence of either C1s, C1q or C1qs during labeling reduced the C1r H-chain label, although C1r remained in the proenzyme form. The presence of C1s or C1rs enhanced the 125I uptake of C1q in Ca2+ or EDTA medium. This was unexpected because one would have anticipated a diminution of the C1q label due to the apposition of C1r and C1s, similarly as it occurs during C1rs complex and C1s dimer formation for the H-chain label of C1s. The results show that C1r and C1q after their conformation during activation and C1 complex formation.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90057-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17330273","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}

引用次数: 11

Influence of calcium binding on the thermal stability of ‘thermitase’, a serine protease from Thermoactinomyces vulgaris 钙结合对普通热放线菌丝氨酸蛋白酶热裂酶热稳定性的影响

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90044-1

Cornelius Frömmel, Wolfgang E. Höhne

引用次数: 37

Isoelectric forms of bacteriorhodopsin from Halobacterium halobium 等电形式的细菌视紫红质

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90045-3

James J. Plantner, Edward L. Kean

引用次数: 7

Effect of α-actinin on actin structure Actin ATPase activity α-肌动蛋白对肌动蛋白结构的影响

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90041-6

Inderjit Singh , Darrel E. Goll , R.M. Robson

{"title":"Effect of α-actinin on actin structure Actin ATPase activity","authors":"Inderjit Singh , Darrel E. Goll , R.M. Robson","doi":"10.1016/0005-2795(81)90041-6","DOIUrl":"10.1016/0005-2795(81)90041-6","url":null,"abstract":"<div>α-Actinin increases the ATPase activity of actin by up to 84%, depending on pH, divalent cations present and the added Mg2+: ATP ratio. Dithiothreitol decreases actin ATPase activity approx. 20% but does not reduce the ability of α-actinin to increase actin ATPase activity. Increasing amounts of added α-actinin up to 1 mol α-actinin to 49 mol actin cause an increasing increment in actin ATPase activity, but adding α-actinin beyond 1 mol α-actinin to 49 mol actin elicits only small additional increments in activity. Actin ATPase activity ranges from approx 100 nmol Pi/mg actin per h (4.3 mol Pi/mol actin per h) at high levels (10 mM) of ATP in the presence of lower amounts (1 mM) of added Mg2+ to approx. 12.5 nmol Pi/mg actin per h (0.52 mol Pi/mol actin per h) at high pH (8.5) or at low levels (0.5–1.0 mM) of ATP in the presence of higher amounts (10 mM) of added Mg2+. ATP uncomplexed with Mg2+ inhibits the ability of α-actinin to increase F-actin ATPase activity. Activities with different divalent cations showed that the actin ATPase in these studies, which was 1/100 as great as Mg2+-modified actomyosin ATPase activity, was not due to trace amounts of myosin contaminating the actin preparations. The results are consistent with the concept that α-actinin can alter the structure of actin monomers.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90041-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17515195","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}

引用次数: 5

Isolation, characterization and localization of A 45 000 molecular weight, soluble glycoprotein from the lung in pulmonary alveolar proteinosis 肺泡蛋白沉积症患者肺可溶性糖蛋白A的分离、鉴定和定位

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90054-4

Robert H. Glew , John U. Balis , Sue Shelley , Theresa Kuhlenschmidt , Ronald Jaffe

{"title":"Isolation, characterization and localization of A 45 000 molecular weight, soluble glycoprotein from the lung in pulmonary alveolar proteinosis","authors":"Robert H. Glew , John U. Balis , Sue Shelley , Theresa Kuhlenschmidt , Ronald Jaffe","doi":"10.1016/0005-2795(81)90054-4","DOIUrl":"10.1016/0005-2795(81)90054-4","url":null,"abstract":"<div>A carbohydrate-rich, water-soluble glycoprotein has been isolated in pure form from delipidated lung lavage fluid from a patient with pulmonary alveolar proteinosis, in a three-step procedure involving ion-exchange and gel filtration chromatography. The molecular weight of the glycoprotein was determined to be 45 900 by sedimentation equilibrium analysis in the analytical ultracentrifuge and 45 000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, indicating a single polypeptide chain. Nearly half of the mass of the glycoprotein is comprised of carbohydrate that is contributed by 24 residues sialic acid, 23 residues N-acetylglucosamine, 6 residues N-acetylgalactosamine, 19 residues galactose, 4 residues mannose, 1 residue fucose and 1 residue glucose per mol. Unlike a number of collagen-related glycoproteins that have been isolated by others from insoluble lung contents in pulmonary proteinosis, the water-soluble glycoprotein described in the present report does not contain hydroxyproline or hydroxylysine and contains less than 10% of its amino acid residues as glycine. Using rabbit antibodies directed against our purest preparation of material and an immunoperoxidase staining procedure, the 45 000 molecular weight glycoprotein was localized to the thin film of fluid lining the surfaces of alveoli in normal human lungs.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90054-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18071209","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}

引用次数: 5

Effect of α-actinin on actin structure Release of bound nucleotide α-肌动蛋白对肌动蛋白结构释放结合核苷酸的影响

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90042-8

Margaret C. Craig-Schmidt , Richard M. Robson , Darrel E. Goll , M.H. Stromer

{"title":"Effect of α-actinin on actin structure Release of bound nucleotide","authors":"Margaret C. Craig-Schmidt , Richard M. Robson , Darrel E. Goll , M.H. Stromer","doi":"10.1016/0005-2795(81)90042-8","DOIUrl":"10.1016/0005-2795(81)90042-8","url":null,"abstract":"<div>We have examined the α-actinin-F-actin interaction by measuring the effect of highly purified α-actinin on bound nucleotide exchange in F-actin. Exchange was followed by measuring the release of actin-bound [14C]ADP in the presence of ATP using an ultrafiltration technique. α-Actinin increases by about 60 to 70% the rate of release of F-actin bound nucleotide when incubated for 1 h in the presence of 1 mM ATP/1 mM MgCl2/0.05 mM CaCl2/0.5 mM dithioerythritol/100 mM KCl/20 mM Tris-acetate, pH 7.5, at 37°C. The ability of α-actinin to enhance nucleotide exchange was maximal when α-actinin was added at a level near 10% of actin present by weight (molar ratio of 1 α-actinin to 49 actin monomers). The potentiating effect of α-actinin on the nucleotide exchange rate of F-actin was not highly related to the Mg2+: ATP ratio present in the incubation mixture. α-Actinin also increased the rate of bound nucleotide exchange of F-actin when the actin was present in a reconstituted actomyosin suspension. The results are consistent with the possibility that one α-actinin can affect the structure of multiple actin monomers present in an actin filament.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90042-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18285287","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}

引用次数: 9

Systematic variation in bond lengths of peptides 多肽键长度的系统性变化

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90058-1

P. Chakrabarti, K. Venkatesan, U. Chandra Singh, C.N.R. Rao

引用次数: 0

Purification and characterisation of the cyclic amp-dependent protein kinase, the C- and the R-protein from bovine liver 牛肝环腺苷依赖性蛋白激酶C-和r -蛋白的纯化和鉴定

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90047-7

Manfred Vogel, Fritz Heinz

{"title":"Purification and characterisation of the cyclic amp-dependent protein kinase, the C- and the R-protein from bovine liver","authors":"Manfred Vogel, Fritz Heinz","doi":"10.1016/0005-2795(81)90047-7","DOIUrl":"10.1016/0005-2795(81)90047-7","url":null,"abstract":"<div>A cyclic AMP-dependent protein kinase, its regulatory (R) and catalytic (C) protein were isolated from bovine liver. The cyclic AMP-dependent protein kinase showed two protein bands on SDS-polyacrylamide gel electrophoresis with molecular weights of 54 000 and 40 000. They correspond to the data for the separately isolated R- and C-protein. The molecular weight of the holoenzyme ranged from 172 000–179 000, depending on the estimation method. The molecular weight of the R-protein ranged from 97 000–98 000. This, and the results of the SDS-polyacrylamide gel electrophoresis, demonstrates a dimeric structure. The frictional ratios (<math><mtext>f</mtext><mtext>f</mtext><msub><mi></mi><mn>0</mn></msub></math>) of 1.67–1.7 for the holoenzyme and 1.9 for the R-protein correspond to highly asymmetric shapes. Assuming a prolate form, the axial ratios are 13–14 and 17, respectively. The C-protein is globular (<math><mtext>f</mtext><mtext>f</mtext><msub><mi></mi><mn>0</mn></msub></math> 1.1–1.26, axial ratio 3–5). The seondary structure with 35% α-helix, 19% β-sheet and 49% aperiodic form of the holoenzyme is similar to the R-protein with 35, 19 and 46%, respectively. The C-protein contains 29% α-helix, 21% β-sheet and 50% aperiodic form. The dimeric R-protein binds 4 mol cyclic AMP and can be phosphorylated in the presence of the C-protein. An absorption coefficient, A280nm1.0%, of 5.4 was calculated for the R-protein and of 13.6 for C-protein. The data for C-protein, e.g., molecular weight, heterogeneity in isoelectrofocusing, phosphate content, etc., are in good agreement with those found by Sudgen, P.H. and Corbin, J.D. (1976) Biochem. J. 159, 423–437.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90047-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17330274","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}

引用次数: 2

The three-iron cluster in a ferredoxin from Desulphovibrio gigas A low-temperature magnetic circular dichroism study 脱硫弧菌铁氧还蛋白中的三铁簇低温磁圆二色性研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90053-2

Andrew J. Thomson , A.Edward Robinson , Michael K. Johnson , Jose J.G. Moura , Isobel Moura , Antonio V. Xavier , Jean Legall

{"title":"The three-iron cluster in a ferredoxin from Desulphovibrio gigas A low-temperature magnetic circular dichroism study","authors":"Andrew J. Thomson , A.Edward Robinson , Michael K. Johnson , Jose J.G. Moura , Isobel Moura , Antonio V. Xavier , Jean Legall","doi":"10.1016/0005-2795(81)90053-2","DOIUrl":"10.1016/0005-2795(81)90053-2","url":null,"abstract":"<div>Ferredoxin II from Desulphovibrio gigas is a tetrameric protein containing a novel iron-sulphur cluster consisting of three iron atoms. The low-temperature magnetic circular dichroism (MCD) spectra of the oxidized and dithionite-reduced forms of ferredoxin II have been measured over the wavelength range approx. 300–800 nm. Both oxidation levels of the cluster are shown to be paramagnetic, although only the oxidized form gives an EPR signal. MCD magnetization curves have been constructed over the temperature range approx. 1.5–150 K and at fields between 0 and 5.1 Tesla. The curve for the oxidized protein can be fitted to a ground state of spin <math><mtext>S = </mtext><mtext>1</mtext><mtext>2</mtext></math> with an isotropic g factor of 2.01. There is evidence for the thermal population of a low-lying electronic state above 50 K. The reduced protein gives a distinctive set of magnetization curves that are tentatively assigned to a ground state of S = 2, with a predominantly axial zero-field distortion that leaves the doublet Ms = ±2 lowest in energy. The zero-field components have a maximum energy spread of approx. 15 cm−1. which places an upper limit of 4 cm−1 on the axial zero-field parameter D. The MCD spectra of the oxidized and reduced forms of the cluster are quite distinctive from one another. The spectra of the oxidized state are also different from those of oxidized high-potential iron protein from Chromatium and should provide a useful criterion for distinguishing between four- and three-iron clusters in their highest oxidation levels.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90053-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17330276","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}

引用次数: 58

Amphitrite ornata erythrocruorin II. Molecular controls of function 两栖藓属红血球蛋白II。功能的分子控制

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90052-0

Emilia Chiancone , Giulia Ferruzzi , Celia Bonaventura , Joseph Bonaventura

{"title":"Amphitrite ornata erythrocruorin II. Molecular controls of function","authors":"Emilia Chiancone , Giulia Ferruzzi , Celia Bonaventura , Joseph Bonaventura","doi":"10.1016/0005-2795(81)90052-0","DOIUrl":"10.1016/0005-2795(81)90052-0","url":null,"abstract":"<div>In the marine terebellid worm Amphitrite ornata the vascular fluid contains a high molecular weight erythrocruorin, while cells of the coelom contain a monomeric hemoglobin. The structural integrity of the erythrocruorin molecule is known to be dependent on the presence of a minimal concentration of divalent cations (1–3 mM) in the medium. The functional properties of Amphitrite erythrocruorin are also affected by cations. The oxygen affinity tends to increase with increasing cation concentration and the degree of cooperative interactions, expressed in the kinetics and equilibria of ligand binding, goes through a maximum. Maximal Hill coefficients of 3–4 are observed with 50 mM CaCl2, 50 mM MgCl2 or 1 M NaCl in measurements at the physiological pH of 7.75. Only 2 mM CaCl2 is required for maximal cooperativity at pH 8.5. This suggests partial deprotonation of the cation binding site at high pH. It is somewhat unusual that pH effects on cooperativity are reversible, since this is not a common feature of the giant erythrocruorin molecules. The oxygen binding experiments revealed a marked effect of divalent cations of Amphitrite erythrocruorin at high pH and cation concentration. Above pH 8.5, at 50 mM CaCl2 and 12°C, the erythrocruorin will form a polymer upon deoxygenation. This polymerization is readily reversible by bringing the temperature from 12 to 20°C or by oxygenation. Under physiological conditions of pH and cation concentration and at 12°C, the ervthrocruorin and the monomeric coelomic hemoglobin require a similar oxygen pressure for half saturation. However, the allosteric regulation of function is absent for the coelomic protein.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90052-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18285286","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}

引用次数: 32