Biochimica et Biophysica Acta (BBA) - Protein Structure最新文献_第5页

Circular dichroism study of horse colipase interaction with bile salt 马胶原酶与胆盐相互作用的圆二色性研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90101-X

Paul Canioni , Robert Julien , Robert Romanetti , Patrick Cozzone , Louis Sarda

{"title":"Circular dichroism study of horse colipase interaction with bile salt","authors":"Paul Canioni , Robert Julien , Robert Romanetti , Patrick Cozzone , Louis Sarda","doi":"10.1016/0005-2795(81)90101-X","DOIUrl":"10.1016/0005-2795(81)90101-X","url":null,"abstract":"<div><p>CD studies have been carried out on horse pancreatic colipases which contain a tryptophan in place of the phenylalanine found at position 52 in the pig protein. From the CD spectra of native proteins in the far ultraviolet region, it was estimated that the secondary structure consists of equal amounts of β-structure and aperiodic arrangements. Colipases contain no α-helical structure. The CD spectra of horse and pig colipases display a positive band at 226 nm the pH dependence of which is characteristic of aromatic chromophores. The near ultraviolet region of the CD spectra of horse and pig colipases contains well-resolved bands at 283–284 nm and 277–278 nm, which corresponds to the tyrosines, with one band at 266–268 nm and one shoulder at 261–263 nm reflecting the contribution of the phenylalanine residues. Comparative analysis of the contribution of sidechains in the aromatic region of the spectra is consistent with a lower solvent accessibility of the lone tryptophan of horse colipase B as compared to isocolipase A. Study of the near ultraviolet CD spectrum of colipase B in the presence of micellar concentration of sodium taurodeoxycholate reveals that the tryptophan (Trp<sub>52</sub>) moves towards a more hydrophobic environment upon the formation of the colipase-bile salt complex. These results support the conclusion that this residue belongs to the previously identified hydrophobic domain of the colipase molecule which interacts with organized lipids (lipid binding site). The conservative substitution of this residue for a phenylalanine in the pig protein suggests that the aromatic structure might be of critical importance for the binding of colipase to the lipid-water interface.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 3","pages":"Pages 305-311"},"PeriodicalIF":0.0,"publicationDate":"1981-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90101-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18309179","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

The purification, N-terminal amino acid sequence and some other properties of an αM-subunit of legumin from the pea (Pisum sativum L.) 豌豆中一个α m亚基的纯化、n端氨基酸序列及其它性质研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90117-3

R. Casey, J.F. March, J.E. Sharman, M.N. Short

引用次数: 18

Evidence for protein self-association induced by excluded volume Myoglobin in the presence of globular proteins 在球状蛋白存在的情况下，排除体积肌红蛋白诱导蛋白自结合的证据

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90103-3

Jacob Wilf, Allen P. Minton

引用次数: 73

Protein rotation, enzyme activity and photooxidation of SH groups in sarcoplasmic reticulum Ca2+-ATPase 肌浆网Ca2+- atp酶中SH基团的蛋白质旋转、酶活性和光氧化

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90118-5

Colin J. Restall, Jose Luis R. Arrondo, Douglas A. Elliot, Anna Jaśkowska, Wilfred V. Weber, Dennis Chapman

{"title":"Protein rotation, enzyme activity and photooxidation of SH groups in sarcoplasmic reticulum Ca2+-ATPase","authors":"Colin J. Restall, Jose Luis R. Arrondo, Douglas A. Elliot, Anna Jaśkowska, Wilfred V. Weber, Dennis Chapman","doi":"10.1016/0005-2795(81)90118-5","DOIUrl":"10.1016/0005-2795(81)90118-5","url":null,"abstract":"<div><p>The binding of probe molecules such as fluorescein isothiocyanate, eosin isothiocyanate and erythrosin isothiocyanate to the Ca<sup>2+</sup>-ATPase of sarcoplasmic reticulum followed by illumination of the labelled protein causes substantial reductions of ATPase activity over a 1-h period. The degree of light-sensitivity induced by these probes is related to the triplet yield of these probe molecules. Consistent with this, the greatest effect is seen with erythrosin isothiocyanate and the least effect with fluorescein isothiocyanate. These reductions of ATPase activity associated with illumination are also associated with an aggregation of the protein molecules. This is indicated by laser flash photolysis measurements and also by polyacrylamide gel electrophoresis. A reduction in the number of thiol groups present on the ATPase molecule parallels the reduction of enzyme activity and changes in the protein mobility. The results are discussed in relation to the use of these probe molecules to study biological systems and also in terms of oxidative processes which may affect protein function in vivo.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 3","pages":"Pages 433-440"},"PeriodicalIF":0.0,"publicationDate":"1981-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90118-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17514524","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: 17

Sarcoplasmic calcium-binding proteins in insect muscle Isolation and properties of locust calmodulin 昆虫肌肉中肌浆钙结合蛋白的分离及蝗虫钙调蛋白的性质

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90119-7

Jos A. Cox, Robert H. Kretsinger , Eric A. Stein

引用次数: 23

Hollow cylinder protein in the cytoplasm of human erythrocytes 人红细胞细胞质中的空心柱状蛋白

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90111-2

Harry L. Malech, Vincent T. Marchesi

{"title":"Hollow cylinder protein in the cytoplasm of human erythrocytes","authors":"Harry L. Malech, Vincent T. Marchesi","doi":"10.1016/0005-2795(81)90111-2","DOIUrl":"10.1016/0005-2795(81)90111-2","url":null,"abstract":"<div><p>A ‘Hollow Cylinder Protein’ (HCP) similar to the protein originally isolated by Harris from human erythrocyte membranes (Harris, J.R. (1968) Biochim. Biophys. Acta 150, 534–537) is present in the cytosol of erythrocytes at a concentration of more than 15 μg/ml packed erythrocytes. When negatively stained and examined in the electron microscope, cytosol HCP is similar in morphology to the HCP associated with erythrocyte ghost membranes. Cytosol HCP can be purified by isoelectric precipitation at pH 5.2 followed by repeated sucrose gradient centrifugation at alkaline pH. Negatively stained purified cytosol HCP appears as a hollow cylinder with apparent dimensions of 18.0 nm in length by 11.8 nm in diameter and contains a hollow core. Purified cytosol HCP migrates as a single band by non-denaturing polyacrylamide gel electrophoresis. SDS-polyacrylamide gel electrophoresis shows that it is composed of five peptides having apparent molecular weights 21 500, 23 500, 26 000, 27 500 and 29 000. Chymotryptic peptide maps of each of these bands indicate that each is a unique polypeptide chain. These results indicate that erythrocyte cytosol HCP is a macromolecular complex composed of multiple copies of five non-identical subunits arranged as a hollow cylinder.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 3","pages":"Pages 385-392"},"PeriodicalIF":0.0,"publicationDate":"1981-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90111-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17945451","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: 13

The hexa- and pentapeptide extension of proalbumin I. Chemical synthesis of serum albumin propeptides 白蛋白原的六肽和五肽延伸。血清白蛋白前肽的化学合成

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90115-X

Chr. Birr , K. Weigand , A. Turan

{"title":"The hexa- and pentapeptide extension of proalbumin I. Chemical synthesis of serum albumin propeptides","authors":"Chr. Birr , K. Weigand , A. Turan","doi":"10.1016/0005-2795(81)90115-X","DOIUrl":"10.1016/0005-2795(81)90115-X","url":null,"abstract":"<div><p>The proalbumin hexapeptide extension was synthesized beginning from the C-terminal end by stepwise N-terminal peptide chain elongation starting from <span><math><mtext>N-tert-</mtext><mtext>butyloxycarbonyl</mtext><mtext>-(N</mtext><msup><mi></mi><mn>g</mn></msup><mtext>-</mtext><mtext>nitro)arginyl</mtext><mtext>-(N</mtext><msup><mi></mi><mn>g</mn></msup><mtext>-</mtext><mtext>nitro)arginine</mtext></math></span> 4-nitrobenzyl ester; <span><math><mtext>[α]</mtext><msub><mi></mi><mn>365</mn></msub><msup><mi></mi><mn>20</mn></msup><mtext>-12°</mtext><mtext>C</mtext></math></span> (<span><math><mtext>c = 1</mtext></math></span>; dimethylformamide). The other amino acids were incorporated by excess mixed anhydrides of Ddz-amino acids (Ddz; 3,5-dimethoxyphenylisopropyloxycarbonyl) yielding the fully protected hexapeptide in crystalline quality. After removal of the protective groups by acid treatment and hydrogenation the peptide was purified by Dowex ion-exchange and Sephadex chromatography. The purity was confirmed by thin-layer chromatography and amino acid analysis.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 3","pages":"Pages 421-423"},"PeriodicalIF":0.0,"publicationDate":"1981-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90115-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17235514","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

The influence of β-93 sulfhydryl groups, organic phosphate and heme concentration on methemoglobin reduction β-93巯基、有机磷酸盐和血红素浓度对高铁血红蛋白还原的影响

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90109-4

Ali Mansouri

{"title":"The influence of β-93 sulfhydryl groups, organic phosphate and heme concentration on methemoglobin reduction","authors":"Ali Mansouri","doi":"10.1016/0005-2795(81)90109-4","DOIUrl":"10.1016/0005-2795(81)90109-4","url":null,"abstract":"<div><p>Native and modified methemoglobin (β-93-SH groups blocked) were reduced by NADH-dependent methemoglobin reductase in the absence and the presence of organic phosphate (inositol hexaphosphate). These experiments were performed with dilute as well as concentrated methemoglobin solutions (physiological heme concentration). It is shown that: (a) in dilute solutions the blockage of β-93-SH groups lowers the rate of methemoglobin reduction in the absence of organic phosphate but the rates of native and modified methemoglobin reduction are similar in the presence of organic phosphate; (b) at physiological heme concentration the blockage of β-93-SH groups does not affect the rate of reduction but the organic phosphate stimulates the reduction of both native and modified methemoglobins in a similar fashion, as it does in dilute solutions. It is concluded that, although in dilute solutions the blockage of β-93-SH groups alters the reduction rate, at physiological heme concentration the presence of free β-93-SH groups does not have any significant effect on methemoglobin reduction. On the contrary, the organic phosphates do accelerate the rate of reduction at all ranges of heme concentration.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 3","pages":"Pages 370-376"},"PeriodicalIF":0.0,"publicationDate":"1981-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90109-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18307367","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: 1

Analysis of pulmonary surfactant apoproteins by electrophoresis 肺表面活性剂载脂蛋白电泳分析

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90104-5

Sikandar L. Katyal, Gurmukh Singh

{"title":"Analysis of pulmonary surfactant apoproteins by electrophoresis","authors":"Sikandar L. Katyal, Gurmukh Singh","doi":"10.1016/0005-2795(81)90104-5","DOIUrl":"10.1016/0005-2795(81)90104-5","url":null,"abstract":"<div><p>Surfactant apoproteins were prepared from detergent-solubilized rat surfactant by immunoaffinity chromatography. SDS-polyacrylamide gel electrophoresis of the apoproteins, without prior chemical reduction, revealed several bands of molecular weights 50 000–78 000, 140 000 and 160 000. Following treatment with dithiothreitol, the apoproteins were resolved into three bands of molecular weights 38 000, 32 000 and 26 000. Further analysis of the apoproteins by two-dimensional polyacrylamide gel electrophoresis showed that each of the proteins of molecular weights 38 000, 32 000 and 26 000 were crosslinked by disulfide bridges and formed homopolymers. Based on periodic acid-Schiff staining, the 38 000 dalton protein appeared to be the richest in carbohydrates, followed by the 32 000 and 26 000 dalton proteins. Partial proteolysis of the 38 000 and 32 000 dalton proteins showed similarity in the sizes of peptides generated. Surfactant-associated proteins from human and monkey lungs were also analyzed by polyacrylamide gel electrophoresis. A non-serum glycoprotein of molecular weight 38 000 was found. In different systems of polyacrylamide gel electrophoresis, this protein showed an electrophoretic mobility similar to that of the 38 000 dalton protein of rat surfactant. However, it formed polymers of molecular weight higher than those of polymers found in rat surfactant.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 3","pages":"Pages 323-331"},"PeriodicalIF":0.0,"publicationDate":"1981-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90104-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17945450","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: 47

X-ray absorption edge spectroscopy of Co(II)-binding sites of copper- and zinc-containing proteins 含铜和含锌蛋白质Co(II)结合位点的x射线吸收边缘光谱

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-10-28 DOI: 10.1016/0005-2795(81)90102-1

A. Desideri , F. Comin , L. Morpurgo , D. Cocco , L. Calabrese , B. Mondovi , W. Maret , G. Rotilio

引用次数: 7