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Protein sequences & data analysis最新文献

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Index of the protein sequences added in 1991 to the Protein Sequence Database of the International Association of Protein Sequence Databanks (PIR-International). 国际蛋白质序列数据库协会(PIR-International) 1991年加入蛋白质序列数据库的蛋白质序列索引。
Protein sequences & data analysis Pub Date : 1993-03-01
{"title":"Index of the protein sequences added in 1991 to the Protein Sequence Database of the International Association of Protein Sequence Databanks (PIR-International).","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 2-4","pages":"67-192"},"PeriodicalIF":0.0,"publicationDate":"1993-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19246669","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: 0
Hydrophobic zippers and hook-and-eye: evolutionarily conserved protein sequence motifs in eukaryotic acidic ribosomal proteins which are assumed to be involved in the association of the protein family. 疏水拉链和钩眼:真核酸性核糖体蛋白中进化上保守的蛋白质序列基序，被认为与蛋白质家族的关联有关。
Protein sequences & data analysis Pub Date : 1992-01-01
K Tsurugi
{"title":"Hydrophobic zippers and hook-and-eye: evolutionarily conserved protein sequence motifs in eukaryotic acidic ribosomal proteins which are assumed to be involved in the association of the protein family.","authors":"K Tsurugi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The acidic ribosomal protein family of eukaryotic cells is thought to form a complex on ribosomes mainly by hydrophobic forces. To investigate the structural basis of how they associate with one another, the primary sequences of the related proteins accumulated from various organisms were analyzed searching for evolutionarily conserved hydrophobic motifs. Initially it is shown that all the P1-type 13-kDa proteins contain a bilateral hydrophobic zipper on a putative alpha-helix, which consists of two periodic arrays of hydrophobic amino acid residues arranged on the opposite sides of an alpha-helix. The P2-type 13-kDa proteins, except for those from the yeast Saccharomyces cerevisiae, are shown to contain two kinds of hydrophobic areas on putative alpha-helices, which can sterically bind to each other in a hook-and-eye fashion. On the other hand, the 38-kDa proteins contain a hydrophobic zipper and a hydrophobic hook in different helical regions. Thus, it is proposed that the 13-kDa proteins associate with the 38-kDa proteins via the hydrophobic zipper or hydrophobic hook-and-eye, and associate with one another with these hydrophobic elements.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"33-8"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12660937","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: 0
A review of cytokine structures. 细胞因子结构研究进展。
Protein sequences & data analysis Pub Date : 1992-01-01
E Minasian, N A Nicola
{"title":"A review of cytokine structures.","authors":"E Minasian,&nbsp;N A Nicola","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The expanding family of cytokines, interleukins and colony-stimulatory factors has made it difficult to readily access their structural and biological properties for comparative purposes. Here their aligned amino acid sequences, biological actions and some structural predictions are presented together for ready comparisons</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"57-64"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12661564","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: 0
Amino acid sequences of ferredoxins from Alocasia macrorrhiza Schott in Papua New Guinea. 巴布亚新几内亚巨根海苔铁氧还毒素的氨基酸序列。
Protein sequences & data analysis Pub Date : 1992-01-01
K Wada, H Sakai, R Masui, M Ihara, H Matsubara
{"title":"Amino acid sequences of ferredoxins from Alocasia macrorrhiza Schott in Papua New Guinea.","authors":"K Wada,&nbsp;H Sakai,&nbsp;R Masui,&nbsp;M Ihara,&nbsp;H Matsubara","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The amino acid sequences of ferredoxin isoproteins (Fd A and Fd B) from Alocasia macrorrhiza Schott in Papua New Guinea were determined. They consisted of single polypeptide chains of 97 and 98 residues, respectively, and both Fds had a molecular mass of 10,800 Da. There was an 88% identity between the sequences of the isoproteins (Fd A and Fd B). These sequences were compared with those of the closely related plant Fds and their phylogenetic relationships are discussed.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"13-9"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12660934","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: 0
Complete amino acid sequence of ovine miniplasminogen. 绵羊微纤溶酶原全氨基酸序列。
Protein sequences & data analysis Pub Date : 1992-01-01
J Schaller, C Straub, U Kämpfer, E E Rickli
{"title":"Complete amino acid sequence of ovine miniplasminogen.","authors":"J Schaller,&nbsp;C Straub,&nbsp;U Kämpfer,&nbsp;E E Rickli","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The complete amino acid sequence of ovine miniplasminogen (M(r) 37,662, 343 residues) was determined with the aid of fragments obtained by cleavage with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine and clostripain. The fragments were aligned with overlapping sequences and sequence comparison with miniplasminogens of other species. Sequence comparison with other species (human, bovine, porcine, equine and canine) gave an overall identity of 63% and a similarity of 83%. The dendrogram of the alignment indicates that ovine miniplasminogen has the closest relationship with the bovine (87% identity) and the most distant with the equine (77% identity) species. The close relationship is indicative for the presence of the same structural and functional domains as in the other species. Sequence comparison of different miniplasminogens showed that positions 49 (Arg), 83 (Arg) and 161 (Ser) in the light chain of the plasmin molecule may play a role in the interaction between plasminogen and streptokinase.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"21-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12660935","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: 0
Purification and characterization of the major cationic kallikrein inhibitor in bovine pituitary gland. 牛脑垂体主要阳离子激肽肽抑制剂的纯化及性质研究。
Protein sequences & data analysis Pub Date : 1992-01-01
M Ikekita, C S Jone, M Kamo, A Tsugita, K Kizuki, H Moriya
{"title":"Purification and characterization of the major cationic kallikrein inhibitor in bovine pituitary gland.","authors":"M Ikekita,&nbsp;C S Jone,&nbsp;M Kamo,&nbsp;A Tsugita,&nbsp;K Kizuki,&nbsp;H Moriya","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The presence of two types of kallikrein inhibitor (cationic and anionic inhibitors) was demonstrated in bovine pituitary gland. These kallikrein inhibitors were separated from the homogenate of bovine posterior pituitary by successive CM-Sephadex chromatography. The major cationic inhibitor was further purified to homogeneity by affinity chromatography using porcine pancreatic beta-kallikrein immobilized on Sepharose 4B and gel filtration. The complete amino acid sequence of this inhibitor was first determined, and it was shown to be a peptide of 58 residues with a calculated molecular weight of 6,511. The Ki value against bovine pituitary kallikrein was 6 x 10(-9) M. The cationic inhibitor was found to be identical with basic pancreatic trypsin inhibitor.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"7-11"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12458257","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: 0
Structural characterization of rabbit brain ubiquitin. 兔脑泛素的结构表征。
Protein sequences & data analysis Pub Date : 1992-01-01
N Wajih, A R Siddiqi, R Kaiser, B Persson, Z H Zaidi, H Jörnvall
{"title":"Structural characterization of rabbit brain ubiquitin.","authors":"N Wajih,&nbsp;A R Siddiqi,&nbsp;R Kaiser,&nbsp;B Persson,&nbsp;Z H Zaidi,&nbsp;H Jörnvall","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ubiquitin has been isolated and purified from rabbit brain using gel permeation and reverse-phase high-performance liquid chromatography. The 76-residue protein exhibits one difference towards a murine form, is identical to other characterized vertebrate ubiquitins, and confirms an extensive conservation of the ubiquitin structure. No positional microheterogeneities were detectable between two sub-forms.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"31-2"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12510855","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: 0
Canine pancreatic kallikrein: enzyme isolation and characterization. 犬胰腺激肽酶的分离与鉴定。
Protein sequences & data analysis Pub Date : 1992-01-01
N Ohnishi, M Ikekita, Y Atomi, K Kizuki, H Moriya, K Kondo, H Yamada, A Tsugita
{"title":"Canine pancreatic kallikrein: enzyme isolation and characterization.","authors":"N Ohnishi,&nbsp;M Ikekita,&nbsp;Y Atomi,&nbsp;K Kizuki,&nbsp;H Moriya,&nbsp;K Kondo,&nbsp;H Yamada,&nbsp;A Tsugita","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Two forms of canine pancreatic kallikrein, designated as canine pancreatic kallikrein A and B, were separately isolated by ion-exchange, affinity and hydrophobic chromatographies. These enzymes had similar apparent molecular masses, substrate specificities and pH optima. However, kallikrein B was inhibited by soybean trypsin inhibitor, while kallikrein A was not. Both kallikrein A and B were shown by sodium dodecyl sulfate-polyacryl amide gel electrophoresis to consist of two polypeptide chains, designated alpha and beta chains, and binding by disulfide bond(s). The N-terminal amino acid sequences of each alpha and beta chains of kallikrein A and B were determined.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12660933","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: 0
The amino acid sequences of two 13-kDa alpha-amylase inhibitors from the seeds of Sorghum bicolor (L.) Moench. 高粱种子中两个13-kDa α -淀粉酶抑制剂的氨基酸序列Moench。
Protein sequences & data analysis Pub Date : 1992-01-01
C Bloch, M Richardson
{"title":"The amino acid sequences of two 13-kDa alpha-amylase inhibitors from the seeds of Sorghum bicolor (L.) Moench.","authors":"C Bloch,&nbsp;M Richardson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Two inhibitors (SI alpha 4 and SI alpha 5) of the alpha-amylases from insect and mammalian sources were purified from seeds of Sorghum bicolor by saline extraction, precipitation with ammonium sulphate, affinity chromatography on Red Sepharose, and preparative and analytical reverse-phase HPLC on columns of Vydac C18. The complete primary structures of these two inhibitors were determined by automated degradation of the intact, reduced and S-alkylated proteins and by manual 4-N,N-dimethylaminoazobenzene-4-isothiocyanate/phenyl isothiocyanate microsequencing of peptides derived from them following enzyme digests. The amino acid sequences were as follows: SI alpha 4: TVDVTACAPGLAIPAPPLPTCRTFARPRTCGLGGPYGPVDPSPVLKQ- RCCRELAAVPSRCRCAALGFMMDGVDAPLQDFRGCTREMQRIYAVSRLTRAAECNLPTIPGGGCHLSNS PR; and SI alpha 5: ANWCEPGLVIPLNPLPSCRTYMVRRACGVSIGPVVPLPVLKERCCSELEKLV- PYCRCGALRTALDSMMTGYEMRPTCSWGGLLTFAPTIVCYRECNLRTLHGRPFCYALGAEGTTT. Comparisons of these sequences with one another and with those of other proteins in the US National Biomedical Research Foundation Databank indicated that the two Sorghum proteins had significant similarities (21%-42% identity) with the members of the cereal superfamily of enzyme inhibitors.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"27-30"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12660936","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: 0
The superfamily of UvrA-related ATPases includes three more subunits of putative ATP-dependent nucleases. 与uvra相关的atp酶超家族包括三个假定的atp依赖核酸酶亚基。
Protein sequences & data analysis Pub Date : 1992-01-01
E V Koonin, A E Gorbalenya
{"title":"The superfamily of UvrA-related ATPases includes three more subunits of putative ATP-dependent nucleases.","authors":"E V Koonin,&nbsp;A E Gorbalenya","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>It is demonstrated that the amino acid sequences of the products of E. coli genes sbcC and prrC, and bacteriophage P2 gene old encompass the four conserved motifs typical of the superfamily of UvrA-related ATPases. A more pronounced statistically significant similarity was revealed between SbcC protein, bacteriophage T4 endonuclease component gp46 and bacteriophage T5 protein D13. It is suggested that the newly identified members of the superfamily might all be ATPase components of the respective nucleases, and that the reactions catalyzed by these enzymes are probably ATP dependent.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"5 1","pages":"43-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12660939","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: 0
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