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  • 1
    Electronic Resource
    Electronic Resource
    L-Asparaginase form Proteus vulgaris. Purification, crystallization, and enzymic properties (1972)
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 217-222 
    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/bi00752a012
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  • 2
    Electronic Resource
    Electronic Resource
    L-Asparaginase from Proteus vulgaris. Subunit and amino acid composition (1973)
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 1075-1079 
    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/bi00730a009
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  • 3
    Electronic Resource
    Electronic Resource
    Involvement of caspase activation through release of cytochrome c from mitochondria in apoptotic cell death of macrophages infected with Actinobacillus actinomycetemcomitans (2004)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 233 (2004), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We previously reported that infection with the periodontopathic bacterium Actinobacillus actinomycetemcomitans induced apoptosis in a mouse macrophage cell line J774.1. In the present study, we examined the involvement of cytochrome c and caspases in the induction of apoptosis in A. actinomycetemcomitans-infected J774.1 cells. Following infection, the expression levels of cytochrome c, and cleaved forms of caspase-3 and caspase-9 in the cells were examined using immunoblot analysis. Cytochrome c was released from mitochondria into the cytoplasm after A. actinomycetemcomitans-infected J774.1 cells were cultured for 6 h, and caspase-3 and caspase-9 were found to be cleaved forms in the cells. Further, caspase-9 activity was markedly increased, and phosphorylated p53 was detected in the cells 30 h following infection. These results suggest that apoptosis in A. actinomycetemcomitans-infected J774.1 cells is regulated by the release of cytochrome c from mitochondria into cytoplasm and the subsequent activation of caspases through phosphorylation of p53.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2004.01.034
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  • 4
    Electronic Resource
    Electronic Resource
    Production of l-alanine from ammonium fumarate using two immobilized microorganisms (1982)
    Springer
    Applied microbiology and biotechnology 15 (1982), S. 147-152 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary For the efficient production of l-alanine from ammonium fumarate using the aspartase activity of immobilized Escherichia coli cells and l-aspartate β-decarboxylase activity of immobilized Pseudomonas dacunhae cells, alanine racemase and fumarase activities should be eliminated. We investigated various procedures to eliminate these side reactions, and found that both activities of intact E. coli cells could be eliminated by treating the culture broth at pH 5.0 and 45° C for 1 h, and those of intact P. dacunhae cells could be eliminated by treating the culture broth at pH 4.75 and 30° C for 1 h. Further, it was confirmed that l-alanine was efficiently produced using these two immobilized pH-treated microorganisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00511238
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  • 5
    Electronic Resource
    Electronic Resource
    Continuous production ofL-malic acid by immobilizedBrevibacterium ammoniagenes cells (1976)
    Springer
    Applied microbiology and biotechnology 3 (1976), S. 169-183 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Continuous production ofL-malic acid from fumaric acid using immobilized microbial cells was investigated. Several microorganisms having fumarase activity were immobilized into a polyacrylamide gel lattice. Among the microorganisms tested, immobilizedBrevibacterium ammoniagenes IAM 1645 showed the highest enzyme activity, but produced an unwanted by-product, succinic acid. Conditions for suppression of this side reaction were investigated, and bile extract treatment of immobilized cells was found to be effective. The bile extract treatment of immobilized cells also resulted in a marked increase of reaction rate forL-malic acid formation. No difference was observed between the native enzyme and immobilized cells in optimal pH and temperature of the enzyme reaction. The effect of temperature on the reaction rate and the stability of fumarase activity of an immobilized cell column were investigated under conditions of continuous enzyme reaction. The decay of enzyme activity during continuous enzyme reaction was expressed by an exponential relationship. Half-life of the fumarase activity of the immobilized cell column at 37°C was calculated to be 52.5 days.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01385432
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  • 6
    Electronic Resource
    Electronic Resource
    Screening of microorganisms having high fumarase activity and their immobilization with carrageenan (1979)
    Springer
    Applied microbiology and biotechnology 7 (1979), S. 161-172 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary To develop an efficient method for continuous production of L-malic acid from fumaric acid using immobilized microbial cells, screening of microorganisms having high fumarase activity was carried out and cultural conditions of selected microorganisms were investigated. As a result of screening microorganisms belonging to the genera Brevibacterium, Proteus, Pseudomonas, and Sarcina were found to produce fumarase in high levels. Among these microorganisms Brevibacterium ammoniagenes, B. flavum, Proteus vulgaris, and Pseudomonas fluorescens were further selected for their high fumarase levels in the cultivation on several media. These 4 microorganisms were entrapped into a k-carrageenan gel lattice, and the resultant immobilized B. flavum showed the highest fumarase activity and operational stability. Cultural conditions for the fumarase formation and the operational stability of fumarase activity of immobilized B. flavum are detailed. Productivity for L-malic acid using immobilized B. flavum with k-carrageenan was 2.3 fold of that using immobilized B. ammoniagenes with polyacrylamide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00505022
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  • 7
    Electronic Resource
    Electronic Resource
    Materials for the fungus flora of Japan (56)Mariannaea camptospora andM. elegans var.punicea from Japan (2000)
    Springer
    Mycoscience 41 (2000), S. 411-414 
    Details
    ISSN: 1618-2545
    Keywords: Mariannaea camptospora ; Mariannaea elegans var.punicea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract One additional species and a variety ofMariannaea, M. camptospora andM. elegans var.punicea, were recorded for the first time in Japan.Mariannaea camptospora formed two types of conidiophores. One type was characterized by simple verticillate phialides sometimes with punctuate walls at the base, producing long oblique conidial chains, and symmetrical spindle-shaped conidia. The other type was characterized by more crowded and shorter phialides with small conidial droplets and hemispherical to concave smaller conidia.Mariannaea elegans var.punicea was characterized by distinct red purple pigmentation in agar media.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02463957
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  • 8
    Electronic Resource
    Electronic Resource
    Continuous production of L-citrulline by immobilized Pseudomonas putida cellsPresented at the Annual Meeting of the Agricultural Chemical Society of Japan, Tokyo, Japan, April 3, 1973. (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1589-1599 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The microbial cells of Pseudomonas putida ATCC 4359 were immobilized by entrapment in a polyacrylamide gel lattice. Enzymatic properties of L-arginine deiminase of the immobilized P. putida cells were investigated and compared with those of the intact cells. The permeability of substrate or product through the cell wall und the heat stability of the enzyme were increased by immobilization of the cells. No difference was observed between pH activity curves of the intact and immobilized cells. The optimal temperature for the formation of L-citrulline was 37°C for the intact cells and 55° C for the immobilized cells.When an aqueous solution of 0.5M L-arginine hydrochloride (pH 6.0) was passed through a column packed with the immobilized cells at a flow rate of SV = 0.26 at 37°C, L-arginine was completely converted to L-citrulline. The enzyme activity of the column was stable and the continuous production of L-citrulline could be carried out at 37°C for the month by using the immobilized cell column. From the effluent of the column, L-citrulline was easily obtained in a good yield.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161203
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  • 9
    Electronic Resource
    Electronic Resource
    Continuous production of urocanic acid by immobilized Achromobacter liquidum cellsPresented at the Annual Meeting of the Society of Fermentation Technology of Japan, Osaka, Japan, November 22,1973. (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1601-1610 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Several microorganisms having higher L-histidine ammonia-lyase activity were immobilized into polyacrylamide gel lattice. The yield of enzyme activity by immobilization was highest in Achromobacter liquidum IAM 1667. As A. liquidum has urocanase activity, the cells were heat-treated at 70°C for 30 min to inactivate the urocanase.Enzymatic properties of the immobilized A. liquidum cells were investigated and compared with those of the intact cells. No difference was observed between the pH activity curve and optimal temperature for the intact and immobilized cells. The permeability of substrate or product through the cell wall was increased by immobilization of the cells.When an aqueous solution of 0.25M L-histidine (pH 9.0) containing 1mM Mg2+ was passed through a column packed with the immobilized A. liquidum cells at a flow rate of SV = 0.06 at 37°C, L-histidine was completely converted to urocanic acid. The L-histidine ammonia-lyase activity of the immobilized cell column was stable over 40 days at 37°C. From the effluent of the immobilized cell column, Urocanic acid was easily obtained in a good yield.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161204
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  • 10
    Electronic Resource
    Electronic Resource
    Continuous production of L-alanine using Pseudomonas dacunhae Immobilized with Carrageenan (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 2045-2054 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Continuous production of L-alanine from L-aspartic acid using immobilized Pseudomonas dacunhae was investigated. Pseudomonas dacunhae cells were immobilized with carrageenan gel. The L-aspartate β-decarboxylase activity of immobilized cells was enhanced by incubating the immobilized cells with a solution of 1M ammonium L-aspartate (pH 5.5) containing 0.1mM pyridoxal-5′-phosphate (PLP) at 37°C over 20 hr. The enzyme activity of immobilized cells was 59% that of intact cells. The pH profile of the enzyme reaction was broader in the immobilized cells than in the free cells. The enzyme activity of immobilized cells was maintained through repeated uses when a substrate solution containing 0.1mM PLP was used. Complete conversion of L-aspartate to L-alanine was attained when a solution of 2M ammonium L-aspartate (pH 6.2) containing 0.1mM PLP was passed upward through the immobilized cell column at a retention time of 8 hr at 37°C. Glutaraldehyde treatment of the immobilized cells resulted in a slight decrease of the enzyme activity but a marked increase of the operational stability. The half-life of enzyme activity was 46 days in glutaraldehyde-treated immobilized cells.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260221005
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