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  • 1995-1999  (8)
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Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Lactobacillus acidophilus Group Lactic Acid Bacteria Applied to Meat Fermentation (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 63 (1998), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Lactobacillus acidophilus group bacteria (L. acidophilus, L crispatus, L. amylovorus, L. gallinarum, L. gasseri, L. johnsonii), probiotic lactic acid bacteria, were applied to meat fermentation. Of six strains, L. gasseri (predominant lacto-bacilli in human intestinal tracts) JCM1131T exhibited greatest fermentation performance in meats. This strain resisted gastric acid and bile, and would thus have no detrimental effects in the intestinal tract. Inoculation of the strain depressed the propagation of S. aureus cells and their enterotoxin production during meat fermentation. Results suggest probiotic lactic acid bacteria could be effectively utilized for meat fermentation to produce healthy meat products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1998.tb15782.x
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  • 2
    Electronic Resource
    Electronic Resource
    Electronic structure of polycrystalline AMoO3 (A=Sr or Ba) (1999)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 85 (1999), S. 6502-6505 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Two strong peaks were observed in the electron energy loss spectra of polycrystalline AMoO3 (A=Sr and Ba) perovskites with metallic conductivities. One, observed at 1.7 eV, was attributed to plasmon loss originating from conduction electrons. This explains the reddish color observed. The other, located at ∼5 eV, was attributed to the charge transfer transition from the Mo4d–O2p bonding band to an unoccupied t2g band through photoemission, ultraviolet inverse photoemission, and x-ray absorption near edge structure spectra. No intense peaks were detected in the energy region between the two absorption bands (2.5〈hν〈3.5 ev), indicating the possibility of application in transparent conductors for the ultraviolet region. © 1999 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.370288
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  • 3
    Electronic Resource
    Electronic Resource
    Production of monoclonal antibody against the C1 component of rat estramustine-binding protein: Immunohistochemical study of rat prostate (1995)
    Springer
    Histochemistry and cell biology 104 (1995), S. 429-433 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The monoclonal antibody against estramustine-binding protein (EMBP) was produced by immunizing a mouse with EMBP antigen purified from rat ventral prostate. On western blotting analysis this antibody recognized the EMBP C1 component, and in an absorption test it recognized the EMBP antigen. Immunohistochemically, this antibody revealed positive staining for the ventral and dorsolateral prostate. In the epithelium of the ventral prostate, intense immunostaining was observed in the intraluminal secretory product; however, in the epithelium of the dorsolateral prostate, the staining was intense in the cytoplasm of the epithelial cells. These findings suggested differences of EMBP localization in the ventral and the dorsolateral prostate. Since the intensity of immunostaining for EMBP was decreased in the prostate of castrated rats, we considered that this antibody reflected the androgen dependency of EMBP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01464332
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  • 4
    Electronic Resource
    Electronic Resource
    Carcinogenesis in accessory sex organs of rats induced by 3,2′-dimethyl-4-aminobiphenyl: response to androgen deprivation (1997)
    Springer
    Histochemistry and cell biology 108 (1997), S. 505-512 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  It is generally accepted that early human prostate cancers reveal higher androgen dependency than do advanced ones. In the present study, we examined whether the animal model of prostate cancer has already lost androgen dependency at the early stages of carcinogenesis. At experimental week 46, androgen deprivation was induced in rats and the incidences of atypical hyperplasia and cancer were examined in the ventral, dorsolateral prostate, coagulating glands, and seminal vesicles. Androgen deprivation significantly lowered the incidence of atypical hyperplasia in all four organs. As for the incidence of cancer, no significant differences were observed in the coagulating glands and seminal vesicles. Regarding atypical hyperplasia, androgen deprivation significantly decreased the proliferative cell nuclear antigen labeling index in the coagulating gland and seminal vesicles. The presence of cancer was also decreased in the coagulating gland but not in the seminal vesicles. With control group specimens, more intense staining of androgen receptor was observed in atypical hyperplasias than in cancers. Compared with the atypical hyperplasias, the cancers revealed low androgen dependency at the early stages of carcinogenesis. The cancers in the seminal vesicles also revealed higher androgen independency than did those in the coagulating gland.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050191
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  • 5
    Electronic Resource
    Electronic Resource
    Enzymatic preparation of optically active 3-trimethylsilylalanine (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 51-55 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  We constructed an efficient system for preparing optically active 3-trimethylsilylalanine (TMS-Ala) by kinetic resolution with acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14). Racemic TMS-Ala was chemically synthesized and acetylated. Enantioselective deacetylation of N-acetyl-DL-TMS-Ala with acylase I from porcine kidney or from Aspergillus melleus was then attempted. Both enzymes could catalyze the deacetylation of N-acetyl-DL-TMS-Ala, and the porcine enzyme was found to have much higher activity than the enzyme from A. melleus. The optimum pH of the porcine-acylase-catalyzed reaction was 7.5, and the addition of 0.5 mM Co2+ accelerated the reaction. Optically pure L-TMS-Ala (〉99% enantiomeric excess, ee) was obtained in 72% yield under the optimized conditions. Furthermore, highly optically pure D-TMS-Ala (96% ee) could also be obtained in 76% yield by chemically hydrolyzing the residual substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050648
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  • 6
    Electronic Resource
    Electronic Resource
    Inhibition of thermolysin by 3-trimethylsilylalanine derivatives (1999)
    Springer
    Applied microbiology and biotechnology 53 (1999), S. 19-22 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The inhibition of thermolysin by an optically active silicon-containing amino acid, 3-trimethylsilylalanine (TMS-Ala), and its derivatives was examined by considering the similarity of structure between TMS-Ala and leucine. Although free l- and d-TMS-Ala did not show the inhibition, several derivatives of l-TMS-Ala, especially Z-l-TMS-Ala and l-Leu-(l-TMS-Ala), exhibited a higher inhibitory activity toward thermolysin than did Z-l-Leu and l-Leu-l-Leu respectively. Effects of TMS-Ala on the activity of its derivatives and the mode of interaction between the derivatives of TMS-Ala and thermolysin are also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051608
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  • 7
    Electronic Resource
    Electronic Resource
    Enzymatic synthesis of silicon-containing dipeptides with 3-trimethylsilylalanine (1999)
    Springer
    Applied microbiology and biotechnology 51 (1999), S. 470-473 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In this study, the enzymatic synthesis of silicon-containing dipeptides with a silicon-containing amino acid, 3-trimethylsilylalanine (TMS-Ala), was attempted in ethyl acetate, and the effects of TMS-Ala on thermolysin-catalyzed dipeptide synthesis are also discussed. Benzyloxycarbonyl(Z)-TMS-Ala was recognized by thermolysin as a better substrate than Z-Leu, and various silicon-containing dipeptides, Z-(TMS-Ala)-Xaa-OMe (Xaa = Leu, Ile, Phe, etc.), could be obtained. The acceleration of the reaction rate in the synthesis of Z-(TMS-Ala)-Leu-OMe compared with Z-Leu-Leu-OMe synthesis was explained by the higher hydrophobicity of the side-chain of TMS-Ala containing a trimethylsilyl group. On the other hand, TMS-Ala-OMe was not accepted as the amino component because of the bulkiness of the trimethylsilyl group. The enantioselectivity of thermolysin was very high. Z-d-TMS-Ala was not a substrate, while Z-l-TMS-Ala served as a good substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051418
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  • 8
    Electronic Resource
    Electronic Resource
    Enzymatic preparation of d-p -trimethylsilylphenylalanine (1997)
    Springer
    Applied microbiology and biotechnology 47 (1997), S. 114-119 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In this paper we report on the enzymatic preparation of d-p-trimethylsilylphenylalanine (d-TMS-Phe). First, dl-5-(p-trimethylsilylphenylmethyl)hydantoin␣(dl-TMS-Phe-Hyd) was synthesized chemically and subjected to bacterial hydrolysis to obtain N-carbamoyl-d-p-trimethylsilylphenylalanine (C-d-TMS-Phe), but no strains examined showed sufficient hydantoinase activity on this compound. However, Blastobacter sp. A17p-4, which is known to produce N-carbamoyl-d-amino acid amidohydrolase (DCase), was found to be able to hydrolyze C-dl-TMS-Phe prepared chemically from the hydantoin. When C-dl-TMS-Phe was hydrolyzed with cells of Blastobacter sp. A17p-4, its optical purity was low because N-carbamoyl-l-amino acid amidohydrolase (LCase) coexisted in the cells. DCase and LCase in the cell-free extract of Blastobacter sp. A17p-4 could be separated by DEAE-Sephacel column chromatography. The optimum pH for the hydrolysis of C-dl-TMS-Phe by the partially purified DCase was 8.0 and addition of 2.5 % N,N-dimethylformamide was effective in raising the substrate concentration without inactivation of DCase. Under the optimized conditions, highly optically pure (98 % enantiomeric excess) d-TMS-Phe could be obtained from C-dl-TMS-Phe with partially purified DCase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050898
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