{"title":"A novel carboxylesterase from Aspergillus niger and its hydrolysis of succinimide esters","authors":"L. Xiaoming, K. Breddam","doi":"10.1007/BF02910459","DOIUrl":"https://doi.org/10.1007/BF02910459","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"35 1","pages":"241-249"},"PeriodicalIF":0.0,"publicationDate":"1989-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85482322","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 signal peptide cleavage site of a B1 hordein determined by radiosequencing of the in vitro synthesized and processed polypeptide","authors":"V. Cameron-Mills, S. Madrid","doi":"10.1007/BF02904472","DOIUrl":"https://doi.org/10.1007/BF02904472","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"42 1","pages":"181-192"},"PeriodicalIF":0.0,"publicationDate":"1989-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78727923","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":"Biosynthesis of Δ-aminolevulinate in Cyanidium caldarium: Characterization of tRNAGlu, ligase, dehydrogenase and glutamate 1-semialdehyde aminotransferase","authors":"J. Houghton, S. Brown, S. Gough, C. Kannangara","doi":"10.1007/BF02907183","DOIUrl":"https://doi.org/10.1007/BF02907183","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"37 1","pages":"131-143"},"PeriodicalIF":0.0,"publicationDate":"1989-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76462059","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":"A new method for the synthesis of glutamate 1-semialdehyde. Characterization of its structure in solution by NMR spectroscopy","authors":"S. Gough, C. Kannangara, K. Bock","doi":"10.1007/BF02908302","DOIUrl":"https://doi.org/10.1007/BF02908302","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"9 1","pages":"99-108"},"PeriodicalIF":0.0,"publicationDate":"1989-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81907379","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":"In situ crosslinking of chlorophyll to protein. Use of specific heterobifunctional photoactivated reagents","authors":"U. Hinz","doi":"10.1007/BF02908304","DOIUrl":"https://doi.org/10.1007/BF02908304","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"6 1","pages":"121-129"},"PeriodicalIF":0.0,"publicationDate":"1989-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78558560","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}
V. Breu, F. Guerbette, J. Kader, C. Gamini Kannangara, B. Svensson, Penny Von Wettstein-Knowles
{"title":"A 10 kD barley basic protein transfers phosphatidylcholine from liposomes to mitochondria","authors":"V. Breu, F. Guerbette, J. Kader, C. Gamini Kannangara, B. Svensson, Penny Von Wettstein-Knowles","doi":"10.1007/BF02907587","DOIUrl":"https://doi.org/10.1007/BF02907587","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"195 1","pages":"81-84"},"PeriodicalIF":0.0,"publicationDate":"1989-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78085682","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 structure and function of the thylakoid membrane","authors":"D. Simpson, D. Wettstein","doi":"10.1007/BF02907585","DOIUrl":"https://doi.org/10.1007/BF02907585","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"67 1","pages":"55-65"},"PeriodicalIF":0.0,"publicationDate":"1989-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83855051","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":"Characterization of a cDNA clone for barley leaf glutamine synthetase.","authors":"S Baima, A Haegi, P Strøman, G Casadoro","doi":"10.1007/BF02910467","DOIUrl":"https://doi.org/10.1007/BF02910467","url":null,"abstract":"<p><p>A barley cDNA clone (1182 bp) encoding chloroplastic glutamine synthetase was isolated with a heterologous cDNA probe of the gene specifying the enzyme from alfalfa. The clone, named pGS8, was found in a lambda gtII cDNA library prepared from dark grown barley leaves even though the chloroplastic glutamine synthetase is absent from such leaves. In agreement therewith the clone hybridized in Northern blot analyses with a 1.7 kb mRNA species present the in poly A+ mRNA fraction of both dark grown and greened primary leaves of barley. The nucleotide sequence of the barley clone reveals 75% identity to the Phaseolus vulgaris and Pisum sativum clones encoding chloroplastic glutamine synthetase, while only 69% identity is observed in comparisons with the clones specifying the cytosolic isozymes. At the amino acid level 85% identity is found between the deduced barley glutamine synthetase sequence and that of the corresponding chloroplastic isoenzymes from bean and pea. The chloroplastic glutamine synthetases contain cysteins in the putative ATP and and substrate binding sites. In the cytosolic forms these positions are occupied by alanine residues.</p>","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"54 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02910467","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13619373","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":"Hybrid bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products.","authors":"R Borriss, O Olsen, K K Thomsen, D von Wettstein","doi":"10.1007/BF02907584","DOIUrl":"https://doi.org/10.1007/BF02907584","url":null,"abstract":"<p><p>Hybrid beta-glucanase genes were constructed by the reciprocal exchange of the two halves of the isolated beta-glucanase genes from Bacillus amyloliquefaciens and B. macerans. The beta-glucanase hybrid enzyme 1 (H1) contains the 107 amino-terminal residues of mature B. amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of B. macerans beta-glucanase. The reciprocal beta-glucanase hybrid enzyme 2 (H2) consists of the 105 amino-terminal residues from the B. macerans enzyme and the carboxyl-terminal 107 amino acids from B. amyloliquefaciens. The biochemical properties of the two hybrid enzymes differ significantly from each other as well as from both parental beta-glucanases. Hybrid beta-glucanase H1 exhibits increased thermostability in comparison to other beta-glucanases, especially in an acidic environment. This hybrid enzyme has maximum activity between pH 5.6 and 6.6, whereas the pH-optimum for enzymatic activity of B. amyloliquefaciens beta-glucanase was found to be at pH 6 to 7 and for B. macerans at pH 6.0 to 7.5. Hybrid enzyme 1 being more heat stable than both parental enzymes represents a case of intragenic heterosis. Hybrid beta-glucanase 2 (H2) was found to be more thermolabile than the naturally occurring beta-glucanases it was derived from and the pH-optimum for enzymatic activity was determined to be between pH 7 and pH 8.</p>","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"54 2","pages":"41-54"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02907584","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13816263","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":"Glycogen phosphorylase: a multifaceted enzyme.","authors":"L N Johnson","doi":"10.1007/BF02910457","DOIUrl":"https://doi.org/10.1007/BF02910457","url":null,"abstract":"","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"54 6","pages":"203-29"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02910457","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13636916","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}