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  • 1
    Electronic Resource
    Electronic Resource
    Probing the combining site of an anti-carbohydrate antibody by saturation-mutagenesis: Role of the heavy-chain CDR3 residues (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 1180-1187 
    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/bi00055a024
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of three distinct Clostridium thermocellum xylanase genes by molecular cloning (1989)
    Springer
    Archives of microbiology 152 (1989), S. 377-381 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium thermocellum ; Xylan ; Xylanase ; Thermostability ; Gene cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three genes coding for xylanase synthesis in Clostridium thermocellum were cloned and expressed in Escherichia coli. Genomic DNA from Clostridium thermocellum was digested to completion with HindIII, BamHI, and SalI. The fragments were ligated into the corresponding sites of pUC19 and transformed into Escherichia coli. Two of the genes encoded for xylanases which depolymerized xylans but were unable to extensively convert these substrates to reducing sugar. The third gene encoded for an enzyme that extensively hydrolyzed xylan. The insert containing the latter gene was subjected to extensive mapping and was found to encode for a xylanase with a molecular weight of approximately 25,000. The protein product of the cloned gene was obtained in a relatively pure form by heat treatment, ion exchange and gel permeation steps. The enzyme was quite stable to high temperatures with a half-life of 24 h at 70°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425176
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  • 3
    Electronic Resource
    Electronic Resource
    Fermentation of xylose and hemicellulose hydrolysates by an ethanol-adapted culture ofBacteroides polypragmatus (1986)
    Springer
    Archives of microbiology 146 (1986), S. 68-73 
    Details
    ISSN: 1432-072X
    Keywords: Bacteroides ; Ethanol ; Xylose ; Hemicellulose ; Fermentation ; Ethanol tolerance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Bacteroides polypragmatus type strain GP4 was adapted to grow in the presence of 3.5% (w/v) ethanol by successive transfers into 1% (w/v)d-xylose media supplemented with increasing concentrations of ethanol. The maximum specific growth rate of the ethanol-adapted culture (μ=0.30 h-1) was not affected by up to 2% (w/v) ethanol but that of the non-adapted strain declined by about 50%. The growth rate of both cultures was limited by nutrient(s) contained in yeast extract. The ethanol yield of the adapted culture (1.01 mol/mol xylose) was higher than that (0.80 mol/mol xylose) of the non-adapted strain. The adapted culture retained the ability to simultaneously ferment pentose and hexose sugars, and moreover it was not inhibited by xylose concentrations of 7–9% (w/v). This culture also readily fermented hemicellulose hydrolysates obtained by mild acid hydrolysis of either hydrogen fluoride treated or steam exploded Aspen wood. The ethanol yield from the fermentation of the hydrolysates was comparable to that obtained from xylose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690161
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  • 4
    Electronic Resource
    Electronic Resource
    Production, crystallization and diffraction to atomic resolution of an antibody Fv specific for the blood-group A oligosaccharide antigen (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 1456-1459 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The histoblood-group ABO carbohydrate antigens are well known as important factors in blood transfusions, but they can also act as receptors for infectious agents and have been implicated in susceptibility to certain carcinomas. A single-chain variable-domain antigen-binding fragment (scFv) gene based on the known sequence of an anti-blood-group-A monoclonal antibody (AC1001) has been synthesized and expressed in Escherichia coli. The purified scFv preparation existed primarily in the monomeric form but also contained large amounts of dimeric and higher oligomeric forms. The corresponding variable-domain antigen-binding fragment (Fv) was generated by cleaving the VL–VH linker with subtilisin, and its activity was demonstrated by surface plasmon resonance with an immobilized bovine serum albumin A–trisaccharide conjugate (KD = 290 µM). AC1001 Fv crystals grown in the presence of N-acetylgalactosamine diffracted to 0.93 Å resolution. This is the first reported example of a crystal of an antibody antigen-binding fragment diffracting to atomic resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998005824
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  • 5
    Electronic Resource
    Electronic Resource
    Germline antibody recognition of distinct carbohydrate epitopes (2003)
    [s.l.] : Nature Publishing Group
    Nature structural biology 10 (2003), S. 1019-1025 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] High-resolution structures reveal how a germline antibody can recognize a range of clinically relevant carbohydrate epitopes. The germline response to a carbohydrate immunogen can be critical to survivability, with selection for antibody gene segments that both confer protection against common ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb1014
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of C λ –C κ Domain Switching on Fab Activity and Yield in Escherichia Coli: Synthesis and Expression of Genes Encoding Two Anti–Carbohydrate Fabs (1994)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 12 (1994), S. 390-395 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] We have used a strategy of hybrid gene synthesis and constant domain shuffling to construct and functionally express in Escherichia coli genes encoding two anti–carbohydrate Fabs, one specific for a Brucella cell–surface polysaccharide and the second for the human blood group A ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0494-390
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  • 7
    Electronic Resource
    Electronic Resource
    Metabolism of Acetivibrio cellulolyticus during optimized growth on glucose, cellobiose and cellulose (1982)
    Springer
    Applied microbiology and biotechnology 16 (1982), S. 212-218 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The growth of Acetivibrio cellulolyticus in 2.5 l batch cultures was optimized by controlling the growth pH at 6.7, the dissolved inorganic sulphide concentration at 0.4–0.6 mM, and by constant removal of hydrogen from the cultures by sparging with N2/CO2 or N2 gas. An initial ethanol concentration of 0.15% (w/v) in cellobiose media resulted in specific growth rates which were reduced by about 75% compared to growth rates of 0.17 h−1 in control cultures. Acetivibrio cellulolyticus had to be adapted for growth on glucose and 14C-radiotracer studies indicated that glucose was metabolized by the Embden-Meyerhof pathway. The specific growth rate (μ=0.03h−1) and molar growth yield (Yglucose=21.5) were considerably lower than those obtained (μ=0.17 h−1, Ycellobiose=68.9) in cellobiose media. A YATP of 12.8 was obtained during growth on cellobiose. The mol product formed per mol Avicel cellulose fermented (on anhydroglucose equivalent basis) were 3.70 H2, 2.64 CO2, 0.73 acetate, 0.39 ethanol and 0.03 total soluble sugars on glucose basis. Maximum cellulase activity was observed in cellulose-grown cultures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00505835
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  • 8
    Electronic Resource
    Electronic Resource
    Properties and potential advantages of β-galactosidase from Bacteroides polypragmatus (1985)
    Springer
    Applied microbiology and biotechnology 22 (1985), S. 114-120 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A β-galactosidase (EC 3.2.1.23) from the mesophilic obligate anaerobe, Bacteroides polypragmatus, was purified 172 fold by p-aminophenyl-β-D-thiogalactopyranoside agarose affinity chromatography followed by Bio-Gel P300 chromatography. The presence of Mg2+ and a reducing agent such as dithiothreitol (DTT) or mercaptoethanol was required for enzyme activity. The optimum pH and temperature, as determined from hydrolysis of the substrate analogue o-nitrophenyl-β-D-galactopyranoside (ONPG), for enzyme activity were 6.8 and 45°C, respectively. There was negligible activity loss during incubation at 35°C for up to 13 h. The Km values obtained with ONPG and lactose as substrates were 0.43 mM and 9.09 mM respectively. The enzyme obtained by affinity chromatography was shown to hydrolyze the lactose component of cheese whey; the amount of lactose hydrolyzed was 32% of that expected with pure lactose as the substrate in buffer containing Mg2+ and DTT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00250030
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  • 9
    Electronic Resource
    Electronic Resource
    Reversibility and competition in the adsorption of Trichoderma reesei cellulase components (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 631-637 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Adsorption reversibility and competition between fractionated components of the Trichoderma reesei cellulase system were studied. Specific endoglucanase (EGI), nonspecific endoglucanases (EGII, EGIII), and cellobio-hydrolase (CBHI) were previously grouped according to their hydrolytic function. At 5°C, direct evidence of exchange between adsorbed and free enzyme was obtained for each component using [3H] and [14C] radiolabeled tracers. No release of bound enzymes was detected upon dilution of the free enzyme solution. In simultaneous adsorption of enzyme pairs, CBHI was shown to predominate adsorption. Endoglucanase EGI was preferentially adsorbed over EGII and EGIII. Sequential adsorption studies have shown that interaction between enzyme components largely determines the degree of their adsorption. Evidence suggests that both common and distinct adsorption sites exist and that their occupation depends on which components are involved. Predominance in adsorption by any one of the enzyme components is decreased at 50°C. Light microscopy and monitoring of sugar production during cellulose hydrolysis provided evidence that reduction in the ionic strength decreases the adsorption predominance of CBHI and enhances the synergism between the cellulase components.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330517
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