Biochimica et Biophysica Acta (BBA) - Protein Structure最新文献_第8页

Further studies on the characterization of cylindrin and torin, two extrinsic proteins of the erythrocyte membrane 进一步研究了红细胞膜外源蛋白圆柱蛋白和torin的特性

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90021-0

J.R. Harris, I. Naeem

引用次数: 16

Molecular properties and biosynthesis of major plasma proteins in Bombyx mori 家蚕主要血浆蛋白的分子特性和生物合成

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90013-1

Susumu Izumi , Junko Fujie , Shigeru Yamada , Shiro Tomino

引用次数: 97

Direct renaturation of the dodecyl sulfate complexes of proteins with triton X-100 triton X-100对十二烷基硫酸盐配合物的直接复性研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90009-X

Steven Clarke

引用次数: 14

Functional studies of two new abnormal hemoglobins with their mutation located at intersubunit contacts: Hb hotel dieu β99 (G1) Asp → Gly and Hb pitie salpetriere β34 (B16) Val → Phe 两种亚基间接触突变的新异常血红蛋白:Hb hotel dieu β99 (G1) Asp→Gly和Hb pittie salpetriere β34 (B16) Val→Phe的功能研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90018-0

Joëlle Thillet, Nicole Arous, Jean Rosa

引用次数: 9

A comparison of the actions of trypsin and pepsin on porcine immunoglobulin M and their effects on biological activity 胰蛋白酶和胃蛋白酶对猪免疫球蛋白M作用的比较及其对生物活性的影响

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90014-3

D. Beale, J.K. Fazakerley

{"title":"A comparison of the actions of trypsin and pepsin on porcine immunoglobulin M and their effects on biological activity","authors":"D. Beale, J.K. Fazakerley","doi":"10.1016/0005-2795(81)90014-3","DOIUrl":"10.1016/0005-2795(81)90014-3","url":null,"abstract":"<div>The action of trypsin at 55°C and pH 8.3 on pig IgM anti-Salmonella has been compared with the action of pepsin at 37°C and pH 4.6. Both processes cause the gradual removal of Fab arms and Cμ2 domains to produce eventually an (Fc)5 fragment. However, during tryptic digestion Fab arms are preferentially removed from the same subunit, whereas peptic digestion causes random removal from any subunit. At intermediate stages of digestion both processes produce partially fragmented molecules which consist of an (Fc)5 portion still attached to limited numbers of Fab arms. Both processes cause a gradual decrease in the ability of molecules to agglutinate Salmonella, but complement fixation by the complexes declines much more rapidly. A stage is reached where molecules having four Fab arms can still agglutinate but there is no complement fixation. However, the remaining arms on the tryptic molecules are distributed in pairs on the same subunit, whereas those on the peptic molecules are distributed randomly. Hence the number of remaining Fab arms, rather than their distribution, appears to be the critical factor which influences biological activity. A possible explanation for this is discussed.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90014-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17846198","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

Covalent immobilization of proteins to N-hydroxysuccinimide ester derivatives of agarose 琼脂糖n -羟基琥珀酰亚胺酯衍生物共价固定化蛋白质

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90004-0

Russell G. Frost, James F. Monthony, Sheldon C. Engelhorn, Christopher J. Siebert

{"title":"Covalent immobilization of proteins to N-hydroxysuccinimide ester derivatives of agarose","authors":"Russell G. Frost, James F. Monthony, Sheldon C. Engelhorn, Christopher J. Siebert","doi":"10.1016/0005-2795(81)90004-0","DOIUrl":"10.1016/0005-2795(81)90004-0","url":null,"abstract":"<div>An uncharged <math><mtext>N-</mtext><mtext>hydroxysuccinimide ester</mtext></math> derivative of agarose, Affi-Gel 10, exhibited excellent capacity for immobilization, at pH 7.5, of proteins having isoelectric points of 6.5–11.0. Under identical conditions, acidic proteins with isoelectric points of 3.3–5.9 did not couple well to this activated gel. Immobilization of acidic proteins increased in the presence of 80 mM CaCl2, or at a pH equal to or less than the isoelectric point. Affi-Gel 15, a new <math><mtext>N-</mtext><mtext>hydroxysuccinimide ester</mtext></math> derivative of agarose containing a tertiary amine in the spacer arm, coupled acidic proteins efficiently at pH 7.5 but basic proteins coupled poorly. The immobilization of basic proteins to Affi-Gel 15 was increased to useful levels by increasing the ionic strength, or the pH, of the reaction medium. The lectin concanavalin A was efficiently immobilized using either activated gel, and the concanavalin A-agarose derivatives bound 3.9–4.1 mg ovalbumin/ml gel. These studies demonstrate that the charge of the protein relative to the charge of the gel is an important factor affecting the level of protein immobilization to active ester gels.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90004-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17235512","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: 19

Phosphorescence of alkaline phosphatase of E. coli in vitro and in situ 大肠杆菌碱性磷酸酶的离体和原位荧光研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90023-4

Toshiharu Horie, Jane M. Vanderkooi

引用次数: 20

Application of high-performance liquid chromatography to abnormal hemoglobin studies 高效液相色谱法在异常血红蛋白研究中的应用

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI: 10.1016/0005-2795(81)90010-6

Jean-Paul Boissel , Henri Wajcman , Hubert Fabritius , Raymond Cabannes , Dominique Labie

引用次数: 15

Physical and chemical characterization of the major lactose-blockable lectin activity from fetal calf skeletal muscle 胎犊骨骼肌中主要乳糖阻断凝集素活性的物理和化学表征

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90055-6

Gaetano T. Montelione , Susan Callahan, Thomas R. Podleski

{"title":"Physical and chemical characterization of the major lactose-blockable lectin activity from fetal calf skeletal muscle","authors":"Gaetano T. Montelione , Susan Callahan, Thomas R. Podleski","doi":"10.1016/0005-2795(81)90055-6","DOIUrl":"10.1016/0005-2795(81)90055-6","url":null,"abstract":"<div>The lactose-blockable lectin activity from fetal calf skeletal muscle has been purified to apparent homogeneity. The purification entails differential centrifugation, ammonium sulfate precipitation, asialofetuin affinity chromatography with a lactose gradient and ion-exchange chromatography on DEAE-cellulose. In the last step, the activity is resolved into a major and minor species, designated ion-exchange-purified lectins I and II, respectively. Both lectin activities are reversibly inhibited by lactose and appear as single bands with identical mobilities on SDSpolyacrylamide gel electrophoresis. Lectin I1 was not obtained in sufficient quantities for further characterization. Lectin I is characterized by a functional requirement for reducing agents and sensitivity to N-ethylmaleimide, which suggests a role for an essential thiol in its activity. Subunit moleculas weight determinations by SDS-polyacrylamide gel electrophoresis (12000 ±1 000) and by gel filtration in 6 M guanidine · HCI (13 000 ± 1 000), when compared with that obtained under native conditions on Bio-Rad P-60 gels (27 000 ± 2 000), suggest a true Mr of 25 000 ± 3 000 for the dimeric molecule. Amino acid composition data, when fitted to this molecular weight, lead to the tentative conclusion that the intact dimer is composed of two very similar but compositionally non-identical chains, designated α and β. While the only detectable N-terminal amino acid is tryptophan, the isoelectric focusing pattern of lectin I supports this heterodimeric structure. In addition, a lactose-insensitive hemagglutinating activity which can be separated from the lactose-blockable activity by affinity chromatography was also observed.</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)90055-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18286313","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: 15

EPR spectral changes of nitrosyl hemes and their relation to the hemoglobin T-R transition 亚硝基血红素的EPR光谱变化及其与血红蛋白T-R转变的关系

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90048-9

Sônia R.W. Louro, Paulo Costa Ribeiro, George Bemski

{"title":"EPR spectral changes of nitrosyl hemes and their relation to the hemoglobin T-R transition","authors":"Sônia R.W. Louro, Paulo Costa Ribeiro, George Bemski","doi":"10.1016/0005-2795(81)90048-9","DOIUrl":"10.1016/0005-2795(81)90048-9","url":null,"abstract":"<div>EPR spectra of nitrosyl hemes were used to study the quaternary structure of hemoglobin. Human adult hemoglobin has been titrated with nitric oxide at pH 7.0 and 25°C. After the equilibration of NO among the α and β subunits the samples were frozen for EPR measurements. The spectra were fitted by linear combinations of three standard signals: the first arising from NO-β-hemes and the other two arising from NO-α-hemes of molecules in the high- and low-affinity conformations. The fractional amounts of α subunits exhibiting the high-affinity spectrum fitted the two-state model (Edelstein, S.J. (1974) Biochemistry 13, 4998–5002) with the allosteric constant L = 7 · 106 and relative affinities cNOα and cNOβ approx. 0.01. Hemoglobin has been marked with nitric oxide at one chain using low-saturation amounts of nitric oxide. The EPR spectra were studied as a function of oxygen saturation. Linear combinations of the three standard signals above fitted these spectra. The fractions of molecules exhibiting the high-affinity spectrum fitted the two-state model with L = 7 · 106, cO2 = 0.0033 and cNOα = 0.08, instead of cNOα = 0.01. Thus, the two-state model is not adequate to describe the conformational transition of these hybrids. The results present evidence of the non-equivalence between oxygen and nitric oxide as ligands.</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)90048-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17330275","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: 21