Carlsberg Research Communications最新文献

A novel carboxylesterase from Aspergillus niger and its hydrolysis of succinimide esters 一种新的黑曲霉羧酸酯酶及其对琥珀酰亚胺酯的水解

Carlsberg Research Communications Pub Date : 1989-11-01 DOI: 10.1007/BF02910459

L. Xiaoming, K. Breddam

引用次数: 5

The signal peptide cleavage site of a B1 hordein determined by radiosequencing of the in vitro synthesized and processed polypeptide 对体外合成和加工的多肽进行放射测序，确定B1蛋白的信号肽裂解位点

Carlsberg Research Communications Pub Date : 1989-09-01 DOI: 10.1007/BF02904472

V. Cameron-Mills, S. Madrid

引用次数: 8

Biosynthesis of Δ-aminolevulinate in Cyanidium caldarium: Characterization of tRNAGlu, ligase, dehydrogenase and glutamate 1-semialdehyde aminotransferase 钙蓝藻Δ-aminolevulinate的生物合成:tRNAGlu、连接酶、脱氢酶和谷氨酸1-半醛转氨酶的表征

Carlsberg Research Communications Pub Date : 1989-07-01 DOI: 10.1007/BF02907183

J. Houghton, S. Brown, S. Gough, C. Kannangara

引用次数: 15

A new method for the synthesis of glutamate 1-semialdehyde. Characterization of its structure in solution by NMR spectroscopy 合成谷氨酸1-半醛的新方法。用核磁共振光谱法表征其在溶液中的结构

Carlsberg Research Communications Pub Date : 1989-05-01 DOI: 10.1007/BF02908302

S. Gough, C. Kannangara, K. Bock

引用次数: 47

In situ crosslinking of chlorophyll to protein. Use of specific heterobifunctional photoactivated reagents 叶绿素与蛋白质的原位交联。使用特异性异双功能光活化试剂

Carlsberg Research Communications Pub Date : 1989-05-01 DOI: 10.1007/BF02908304

U. Hinz

引用次数: 0

A 10 kD barley basic protein transfers phosphatidylcholine from liposomes to mitochondria 一种10 kD的大麦碱性蛋白将磷脂酰胆碱从脂质体转移到线粒体

Carlsberg Research Communications Pub Date : 1989-03-01 DOI: 10.1007/BF02907587

V. Breu, F. Guerbette, J. Kader, C. Gamini Kannangara, B. Svensson, Penny Von Wettstein-Knowles

引用次数: 56

The structure and function of the thylakoid membrane 类囊体膜的结构和功能

Carlsberg Research Communications Pub Date : 1989-03-01 DOI: 10.1007/BF02907585

D. Simpson, D. Wettstein

引用次数: 31

Characterization of a cDNA clone for barley leaf glutamine synthetase. 大麦叶片谷氨酰胺合成酶cDNA克隆的鉴定。

Carlsberg Research Communications Pub Date : 1989-01-01 DOI: 10.1007/BF02910467

S Baima, A Haegi, P Strøman, G Casadoro

{"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":"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.","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":null,"pages":null},"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}

引用次数: 12

Hybrid bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products. 杂交芽孢杆菌内(1-3,1-4)- β -葡聚糖酶:重组基因的构建及基因产物的分子性质

Carlsberg Research Communications Pub Date : 1989-01-01 DOI: 10.1007/BF02907584

R Borriss, O Olsen, K K Thomsen, D von Wettstein

{"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":"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.","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":null,"pages":null},"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}

引用次数: 49

Glycogen phosphorylase: a multifaceted enzyme. 糖原磷酸化酶:一种多面酶。

Carlsberg Research Communications Pub Date : 1989-01-01 DOI: 10.1007/BF02910457

L N Johnson

引用次数: 5