W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick
{"title":"The following protein sequences were reprinted from the protein sequence database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 1","pages":"21-140"},"PeriodicalIF":0.0,"publicationDate":"1990-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13464486","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":"Amino acid sequence of ferredoxin isolated from Cyanidium caldarium strain RK-1.","authors":"H Nagashima, K Sakai, M Kamo, A Tsugita","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ferredoxin was isolated from ther eukaryotic alga Cyanidium caldarium strain RK-1 and its amino acid sequence was determined. The ferredoxin is composed of 97 amino acid residues, and its molecular weight is 10,599 excluding the iron-sulfur cluster. The amino acid sequence differs from that of C. caldarium strain 1355/1, by 24 amino acid substitutions plus one deletion at the amino terminus.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"457-60"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13768929","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}
S Matuda, K Nakano, T Saheki, R Oyama, M Suzuki, K Titani
{"title":"Determination of partial amino acid sequence of lipoate acetyltransferase of rat pyruvate dehydrogenase complex.","authors":"S Matuda, K Nakano, T Saheki, R Oyama, M Suzuki, K Titani","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The partial amino acid sequence of rat lipoate acetyltransferase was determined using the intact protein and the peptides derived from a digest with Achromobacter protease I. The results showed the amino-terminal sequence of the mature enzyme to be (N) Ser-Leu-Pro-Pro-His-Gln-Lys-Val-Pro-Leu-Pro-Ser- Leu-Ser-Pro-Thr-Met-Gln-Ala-Gly-Thr-Ile-Ala-Arg-Trp-Glu-Lys. In addition, the sequences of two possible lipoyl-binding sites in the subunit, which are very similar to each other, were established.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"441-4"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13837165","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":"High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis.","authors":"J R Beeching","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The deduced amino acid sequences of isocitrate lyase (EC 4.1.3.1) from Escherichia coli and Ricinus communis (castor bean) were compared and regions of high homology between the two enzymes were identified. The castor-bean enzyme had a 14 amino acid amino-terminal, and a 25 amino acid carboxy-terminal extension and a 102 amino acid central insertion compared to the E. coli enzyme. Enzymatic data were used to attempt to identify specific amino acids in the active site. Comparisons with putative peroxisomal/gloxysomal targeting sequences were made and a region including part of the central insertion of the castor bean enzyme was tentatively identified.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"463-6"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13837166","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":"Procarboxypeptidase A activation segment compared to structures of other proteins.","authors":"J Vendrell, B Persson, F X Avilés, H Jörnvall","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The 94-residue activation segment of procarboxypeptidase A was compared with segments of other proteins. No significant homologies were observed towards other activation segments, but an inter-domain segment preceding the serine-protease part of complement factor B showed some structural relationships with the N-terminal region of the procarboxypeptidase A activation segment. This may reflect common functional and organizational patterns. In contrast, the present comparisons do not give functional or further sequence support to previously proposed structural homologies with helix-loop-helix (EF-hand) calcium-binding proteins.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"461-2"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13768930","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}
K Hochstrasser, M Paulus, E Wachter, P W Reisinger
{"title":"The amino-acid sequence of the double-headed proteinase inhibitor from badger (Meles meles) submandibular glands.","authors":"K Hochstrasser, M Paulus, E Wachter, P W Reisinger","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Badger submandibular glands contain a double-headed secretory proteinase inhibitor. Its amino acid sequence was determined. Extensive homologies were found between this inhibitor and the corresponding inhibitors of fox, dog, lion and cat in both domains. As in fox and dog inhibitor, the trypsin-inhibiting domain of badger inhibitor contains an Arg residue in the reactive site in contrast to a Lys residue in the inhibitors of lion and cat. Domains I and II of badger inhibitor are structurally related both to the sequenced inhibitors of fox, dog, lion and cat and to the sequenced monovalent secretory pancreatic trypsin inhibitors. The sequence of the badger inhibitor is N-terminally extended by four amino acids in comparison to fox and dog inhibitors and extended by eight amino acids in comparison to lion and cat inhibitors. Furthermore, the badger inhibitor is C-terminally extended by two amino acids in comparison to the lion inhibitor and by three amino acids in comparison to all other sequenced inhibitors.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"453-6"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13768928","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":"Phospholipase A2 from cobra (Naja naja naja) venom. Primary structure and subspecies variation.","authors":"J Shafqat, O U Beg, H Jörnvall, Z H Zaidi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The primary structure of phospholipase A2 of the major race of Indian cobra has been determined. Together with previous data on other subforms, it establishes subspecies variations at no less than 20 of the 119 positions in the protein. These variations are large, not only in number but in several cases also regarding properties of the residues involved. Nevertheless, all structures are compatible with largely unaltered enzyme properties.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"451-2"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13769012","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}
W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick
{"title":"The following protein sequences were reprinted from the protein sequence database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"467-537"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13768931","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":"Complete amino acid sequence of canine miniplasminogen.","authors":"J Schaller, C Straub, U Kämpfer, E E Rickli","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The complete amino acid sequence of canine miniplasminogen (Mr 36,678, 333 residues) was determined with the aid of fragments obtained by cleavage with BNPS-skatole, cyanogen bromide or clostripain. The fragments were aligned with overlapping sequences. Sequence comparison with miniplasminogens of other species gave identities in the range of 80% (bovine) and 88% (human), indicating the presence of the same structural and functional domains as in the other species. Sequence comparison of different miniplasminogens showed that plasminogens of species activated by streptokinase have identical residues in positions 49, 83 and 161 of the plasmin light chain. The triad of these amino acids may represent at least one of eventually several prerequisites for the interaction and activation of plasminogen with streptokinase.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 6","pages":"445-50"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13769011","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 amino acid sequence of plastocyanin from rice (Oryza sativa, subspecies japonica).","authors":"H Yano, M Kamo, A Tsugita, K Aso, Y Nozu","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The amino acid sequence of plastocyanin from rice (subspecies japonica) was determined. It consists of a single polypeptide chain of 97 residues and has a molecular mass of 10,225 Da. The sequence shows 94.8% identity with barley plastocyanin.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 5","pages":"385-9"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13920691","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}