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  • 1
    Electronic Resource
    Electronic Resource
    The Action on Soluble Blood Group A Substances of an α-N-Acetylgalactosaminidase from Helix pomatia* (1966)
    s.l. : American Chemical Society
    Biochemistry 5 (1966), S. 1742-1747 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00869a042
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  • 2
    Electronic Resource
    Electronic Resource
    Recent advances in the genetics of the clostridia (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 63 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Several laboratories around the world have started work on genetic analysis of clostridia. Interest in this diverse group of anaerobic organisms has grown with increasing awareness of the benefits that may accrue from their biotechnological exploitation. Research to date has focussed on construction of shuttle vectors containing replicons from clostridial and streptococcal plasmids, development of methods for transferring genes, and molecular cloning of genes—especially those involved in toxigenicity, fermentative metabolism and polysaccharide utilization. In selected species gene transfer by protoplast transformation, electroporation and conjugation has been accomplished and transposable elements have been introduced. It can be anticipated that our understanding of the molecular biology of these interesting organisms will grow rapidly in the future, bringing with it improved prospects for rational biotechnological exploitation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03402.x
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  • 3
    Electronic Resource
    Electronic Resource
    Plasmid R1 DNA replication dependent on protein synthesis in cell-free extracts of E. coli (1981)
    [s.l.] : Nature Publishing Group
    Nature 289 (1981), S. 326-328 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1Requirements of the systemc Omissions dCMP incorporated (pmol) None 94.9 MgCl2 0.8 dTTP 5.1 ATP 2.1 CTP, GTP, UTP 3.5 Creatine phosphate 1.0 Cyclic AMP 36.7 Amino acids 40.3 Extract was prepared from C600 (pKN177) and supplemented with exogenous pKN177 DNA (30 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/289326a0
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  • 4
    Electronic Resource
    Electronic Resource
    Microsomal Incorporation of N -Acetyl- D -galactosamine into Blood Group Substance (1966)
    [s.l.] : Nature Publishing Group
    Nature 210 (1966), S. 316-317 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The mechanism of the biosynthesis of blood group substances is unknown. In vivo labelling experiments in which [14C]-glycerol was injected into the gastric artery of hogs indicated that blood group substances are synthesized on the microsomes of the gastric mucosa8. This communication describes the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/210316a0
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  • 5
    Electronic Resource
    Electronic Resource
    Construction ofClostridium butyricum hybrid plasmids and transfer toBacillus subtilis (1985)
    Springer
    Applied microbiology and biotechnology 23 (1985), S. 114-122 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Small plasmids were isolated from type strains ofClostridium butyricum. Strain NCIB 7423 carries one plasmid (pCBU1) of 6.4 kb, whereas strain NCTC 7423 carries two unrelated plasmids of 6.3 kb (pCBU2) and 8.4 kb (pCBU3). Cleavage sites for 18 restriction endonucleases have been mapped on these plasmids and detailed physical maps are presented. For the purpose of developing vector plasmids for gene cloning in saccharolytic clostridia these crypticC. butyricum plasmids were joined to a selectable marker that will likely be expressed in clostridia. This was achieved by cloning the clostridial plasmids into theE. coli vector pBR322 carrying the chloramphenicol acetyltransferase (CAT) gene from theStaphylococcus aureus plasmid pC194. The recombinant plasmids were tested for their ability to confer chloramphenicol resistance toBacillus subtilis. Hybrid plasmids (pHL105, pHL1051) derived from pCBU2 were identified, which are capable of replication and expression of theS. aureus drug resistance marker in bothE. coli andB. subtilis. No structural instability was detected upon retransformation of pHL105 fromB. subtilis intoE. coli. The recombinant plasmids might thus be useful as shuttle vectors for the gene transfer betweenE. coli and a wide range of bacilli and clostridia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982727
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  • 6
    Electronic Resource
    Electronic Resource
    Purification and properties of an extracellular β-glucosidase from the cellulolytic thermophile Clostridium stercorarium (1988)
    Springer
    Applied microbiology and biotechnology 28 (1988), S. 380-386 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Clostridium stercorarium cultures grown on cellobiose contain both an extracellular and a cell-bound β-glucosidase activity. A substantial portion of the cell-bound enzyme could be extracted by osmotic shock, suggesting a periplasmic localization. The β-glucosidase present in culture supernatants was purified to homogeneity. It was found to be identical in all aspects tested with the cell-bound β-glucosidase. The enzyme exists as a monomer with an apparent molecular weight of 85.000 (SDS-PAGE) and a pI of 4.8. It shows optimal activity as pH 5.5 and 65° C. Thiol groups are essential for enzyme activity. In the presence of reducing agents and divalent cations the half-life of the purified enzyme was more than 5 h at 60°C. The enzyme hydrolyses at different rates a wide range of substrates including aryl-β-glucosides, cellobiose, and disordered cellulose. K m values were determined as 0.8 mM for p-nitrophenyl-β-glucoside (PNPG) and 33 mM for cellobiose. The cellular localization and the substrate specificity pattern are consistent with a dual role of the C. stercorarium β-glucosidase in cellulose saccharification: (1) Cleavage of cellobiose formed by exoglucanase and (2) degradation of cellodextrins produced by endoglucanase action.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268200
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  • 7
    Electronic Resource
    Electronic Resource
    High-level expression of Clostridium thermocellum cellulase genes in Escherichia coli (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 50-56 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The Clostridium thermocellum cellulase genes celA and celC encoding endoglucanase A and C were subcloned in a temperature-regulated Escherichia coli expression vector containing the leftward promoterpl of bacteriophage lambda. The level of gene expression was controlled by thermal inactivation of the heat-sensitive lambda cI857 repressor. Under optimal conditions the recombinant endoglucanases A and C were expressed to a level of 10–15% of total cellular protein. Endoglucanase A was partially exported into the periplasmic space, whereas endoglucanase C was found sequestered within the cytoplasm. Overexpression of the celA gene resulted in decreased cell viability concomitant with the accumulation of endoglucanase A in the membrane fraction. In contrast, high-level synthesis of the celC gene product was well tolerated by the host cell. Overproduced endoglucanase C accumulated as a soluble enzyme without detectable formation of inactive inclusion bodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00257253
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  • 8
    Electronic Resource
    Electronic Resource
    Degradation of barley β-glucan by endoglucanase C of Clostridium thermocellum (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 25-31 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Endoglucanase C encoded by the celC gene of Clostridium thermocellum has been purified to homogeneity from a recombinant Escherichia coli strain. It was found that this enzyme is highly efficient in degrading glucans with alternating β-1,4- and β-1,3-linkages but lacks activity on unmodified cellulosic substrates. The properties of endoglucanase C were compared to those of Bacillus subtilis β-glucanase, an enzyme used in the brewing industry for β-glucan degradation. Both enzyme cause a rapid decrease of the viscosity of barley β-glucan as a result of internal chain cleavage. Endoglucanase C hydrolyses non-specifically β-1,3- and β-1,4-bonds adjacent to unsubstituted or 4-O′-substituted cellobiose units. Due to its lower pH optimum and increased thermostability endoglucanase C compares favourably with B. subtilis β-glucanase and seems suitable for use in the mashing process of beer brewing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00258346
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  • 9
    Electronic Resource
    Electronic Resource
    Construction ofClostridium butyricum hybrid plasmids and transfer toBacillus subtilis (1985)
    Springer
    Applied microbiology and biotechnology 23 (1985), S. 114-122 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Small plasmids were isolated from type strains ofClostridium butyricum. Strain NCIB 7423 carries one plasmid (pCBU1) of 6.4 kb, whereas strain NCTC 7423 carries two unrelated plasmids of 6.3 kb (pCBU2) and 8.4 kb (pCBU3). Cleavage sites for 18 restriction endonucleases have been mapped on these plasmids and detailed physical maps are presented. For the purpose of developing vector plasmids for gene cloning in saccharolytic clostridia these crypticC. butyricum plasmids were joined to a selectable marker that will likely be expressed in clostridia. This was achieved by cloning the clostridial plasmids into theE. coli vector pBR322 carrying the chloramphenicol acetyltransferase (CAT) gene from theStaphylococcus aureus plasmid pC194. The recombinant plasmids were tested for their ability to confer chloramphenicol resistance toBacillus subtilis. Hybrid plasmids (pHL105, pHL1051) derived from pCBU2 were identified, which are capable of replication and expression of theS. aureus drug resistance marker in bothE. coli andB. subtilis. No structural instability was detected upon retransformation of pHL105 fromB. subtilis intoE. coli. The recombinant plasmids might thus be useful as shuttle vectors for the gene transfer betweenE. coli and a wide range of bacilli and clostridia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00938963
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  • 10
    Electronic Resource
    Electronic Resource
    Resolution of Clostridium stercorarium cellulase by fast protein liquid chromatography (FPLC) (1988)
    Springer
    Applied microbiology and biotechnology 27 (1988), S. 432-436 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A fast and efficient separation procedure for the analysis of the cellulase components of the thermophilic anaerobe Clostridium stercorarium was developed. Culture respernatants were concentrated without loss of cellulase activity by tangential flow ultrafiltration. Resolution of the cellulase system was achieved by fast protein liquid chromatography (FPLC) on a Mono Q anion exchange column. Enzyme fractions were assayed for hydrolysis of Avicel, carboxymethylcellulose (CMC), β-nitrophenyl-β-d-cellobioside, and p-nitrophenyl-β-d-glucoside. Two Avicelases, two β-cellobiosidases, and one β-glucosidase were identified and characterized by SDS-polyacrylamide electrophoresis and isoelectric focusing. On the basis of their activities towards CMC, Avicelase I was classified as endo-β-glucanase and Avicelase II as exo-β-glucanase. Efficient hydrolysis of microcrystalline cellulose was shown to result from the combined action of both Avicelases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00451608
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