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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 665 (1992), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Knowledge Acquisition 5 (1993), S. 385-403 
    ISSN: 1042-8143
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Computer Science
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1185 (1994), S. 50-55 
    ISSN: 0005-2728
    Keywords: (E. coli) ; ATPase, H^+- ; Product activation ; ε-Subunit
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0196-9781
    Keywords: AVP ; Binding site ; Cortex ; Receptor ; ZNC(C)PR
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 399-404 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  CelS is the most abundant subunit and an exoglucanase component of the Clostridium thermocellum cellulosome, multicomponent cellulase complex. The product inhibition pattern of CelS was examined using purified recombinant CelS (rCelS) produced in Escherichia coli. The rCelS activity on cellopentaose was strongly inhibited by cellobiose. The rCelS activity was also inhibited by lactose. Glucose was only marginally inhibitory. Cellobiose appeared to inhibit the rCelS activity through a competitive mechanism. The inhibition was relieved when β-glucosidase was added, presumably because of the conversion of cellobiose into glucose. These hydrolysis product inhibition patterns are consistent with those of the crude enzyme (cellulosome), suggesting that CelS is a rate-limiting factor in the activity of the cellulosome.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 399-404 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract CelS is the most abundant subunit and an exoglucanase component of the Clostridium thermocellum cellulosome, multicomponent cellulase complex. The product inhibition pattern of CelS was examined using purified recombinant CelS (rCelS) produced in Escherichia coli. The rCelS activity on cellopentaose was strongly inhibited by cellobiose. The rCelS activity was also inhibited by lactose. Glucose was only marginally inhibitory. Cellobiose appeared to inhibit the rCelS activity through a competitive mechanism. The inhibition was relieved when β-glucosidase was added, presumably because of the conversion of cellobiose into glucose. These hydrolysis product inhibition patterns are consistent with those of the crude enzyme (cellulosome), suggesting that CelS is a rate-limiting factor in the activity of the cellulosome.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of plant growth regulation 15 (1996), S. 27-31 
    ISSN: 1435-8107
    Keywords: Ipomoea batatas (L.) Lam ; Calonyction aculeatum (L.) House ; Growth regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Calonyctin, a natural plant growth regulator extracted from the leaves of Calonyction aculeatum (L.) House, can promote crop growth and increase crop yield. The specific reasons for this response are unknown. This study was conducted to determine the effect of calonyctin treatment on the free sugars of sweet potato [Ipomoea batatas (L.) Lam.] as related to starch accumulation. The sweet potatoes were grown in the field in 1992, treated by foliar spray with Calonyctin concentrations of 0 (control) and 0.1 activity unit (CTSP) at 20 days after planting (DAP) at the rate of 190 liters of diluted solution/ha., and sampled periodically to determine free sugars. The response of sweet potato to calonyctin was first detected at 40 days after treatment (on 60 DAP). Data indicated that calonyctin treatment significantly increased starch synthesis in storage roots, decreased the fluctuation tendency of total sugar level during the growth period, and kept the sugar level relatively constant with a gradual rise regardless of variations in weather. The level of the reducing sugars in CTSP leaves was higher at 60 and 160 DAP and lower at 100, 120, and 140 DAP. During rainy days (100 DAP), the reducing sugars in CTSP storage roots remained at a lower level when those in controls reached high levels. The sucrose content in CTSP leaves was 40–138% greater than that in controls except at 80 and 120 DAP, and the ratio of sucrose to total nonreducing sugars remained at 100% in CTSP leaves even on rainy and cool days and above 96% in CTSP storage roots except on cool days (140 and 160 DAP), suggesting that calonyctin treatment promoted the synthesis and transfer of sucrose and supplied abundant sugar precursors for starch accumulation in storage roots.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 42 (1994), S. 346-352 
    ISSN: 1432-0614
    Keywords: Key words Clostridium thermocellum  ;  CellulaseCellulosome  ;  CelS  ;  Exoglucanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Clostridium thermocellum ATCC 27405 produces an extremely complicated multi-component cellulase aggregate (cellulosome) highly active on crystalline cellulose. From the cellulosome, two subunits, CelS (or SS; M r=82 000) and CelL (or SL, CipA; M r=250 000), have been identified as essential for crystalline cellulose degradation [Wu et al. (1988) Biochemistry 27:1703]. We have determined the DNA sequence of the celS gene from four cloned DNA fragments encompassing this gene [Wang et al. (1993) J Bacteriol 175:1293]. To express the entire celS gene in Escherichia coli, the celS structural gene was amplified by the polymerase chain reaction (PCR) employing the PCR primers corresponding to sequences flanking the desired gene. This PCR product (2.1×103 bases; 2.1 kb) was cloned into an E. coli expression vector pRSET B. Subsequent expression of the cloned gene resulted in a fusion protein (rCelS; M r=86 000) as inclusion bodies. The rCelS protein was recognized specifically by an anti-CelS antiserum in a Western blot analysis. The inclusion bodies were purified and solubilized in 5 M urea. The refolded rCelS produced very little reducing sugar from carboxymethylcellulose. However, it showed a higher activity on the crystalline cellulose (Avicel) and an even higher activity on phosphoric-acid-swollen Avicel. These results indicate that the CelS is an exoglucanase.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 42 (1994), S. 346-352 
    ISSN: 1432-0614
    Keywords: Clostridium thermocellum ; Cellulasex ; Cellulosome ; CelS ; Exoglucanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Clostridium thermocellum ATCC 27405 produces an extremely complicated multi-component cellulase aggregate (cellulosome) highly active on crystalline cellulose. From the cellulosome, two subunits, CelS (or S s ;M r = 82 000) and CelL (or S l , CipA;M r = 250 000), have been identified as essential for crystalline cellulose degradation [Wu et al. (1988) Biochemistry 27:1703]. We have determined the DNA sequence of thecelS gene from four cloned DNA fragments encompassing this gene [Wang et al. (1993) J Bacteriol 175:1293]. To express the entirecelS gene inEscherichia coli, thecelS structural gene was amplified by the polymerase chain reaction (PCR) employing the PCR primers corresponding to sequences flanking the desired gene. This PCR product (2.1 x 103 bases; 2.1 kb) was cloned into anE. coli expression vector pRSET B. Subsequent expression of the cloned gene resulted in a fusion protein (rCelS;M r = 86 000) as inclusion bodies. The rCelS protein was recognized specifically by an anti-CelS antiserum in a Western blot analysis. The inclusion bodies were purified and solubilized in 5m urea. The refolded rCelS produced very little reducing sugar from carboxymethylcellulose. However, it showed a higher activity on the crystalline cellulose (Avicel) and an even higher activity on phosphoricacid-swollen Avicel. These results indicate that the CelS is an exoglucanase.
    Type of Medium: Electronic Resource
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