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  • 1
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  During a screening for new microbial α-glucan phosphorylases corynebacteria were found to be promising, not-yet-identified producers of these particular enzymes. A maltodextrin phosphorylase (MDP) from Corynebacterium callunae was isolated, partially characterized, and used for the production of glucose-1-phosphate (G-1-P) from different α-glucans. In fermentor cultivations of C. callunae using maltodextrin as the inducing carbohydrate component, an MDP activity of approximately 8–10 units/g biomass (equivalent to 250 units/l) could be obtained. Contaminating activities of phosphoglucomutase and phosphatase were removed by ammonium sulphate precipitation followed by hydrophobic interaction chromatography on phenyl-sepharose. The partially (14-fold) purified MDP showed pH optima of 6.8 and 6.0 in the direction of phosphorolysis and synthesis, respectively. In the presence of 50 mM inorganic phosphate the enzyme was stable for more than 2 months at room temperature. The new MDP is capable of producing G-1-P from maltodextrins, soluble starch, and glycogen with decreasing order of activity. The same glucans were accepted as primers in the direction of synthesis. Increasing pH values favoured the formation of G-1-P and optimized conditions for its production were established at a pH of 7.5. The maximum attainable yields of G-1-P by the action of MDP are limited by mainly two factors: (1) no more than approximately 20% of the initial inorganic phosphate could be converted into G-1-P and (2) the highest degrees of phosphorolytic maltodextrin degradation were in the range 30–35%. These values could be increased to more than 60% after pretreatment of the maltodextrins with pullulanase.
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  • 2
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract During a screening for new microbial α-glucan phosphorylases corynebacteria were found to be promising, not-yet-identified producers of these particular enzymes. A maltodextrin phosphorylase (MDP) from Corynebacterium callunae was isolated, partially characterized, and used for the production of glucose-1-phosphate (G-1-P) from different α-glucans. In fermentor cultivations of C. callunae using maltodextrin as the inducing carbohydrate component, an MDP activity of approximately 8–10 units/g biomass (equivalent to 250 units/l) could be obtained. Contaminating activities of phosphoglucomutase and phosphatase were removed by ammonium sulphate precipitation followed by hydrophobic interaction chromatography on phenyl-sepharose. The partially (14-fold) purified MDP showed pH optima of 6.8 and 6.0 in the direction of phosphorolysis and synthesis, respectively. In the presence of 50mm inorganic phosphate the enzyme was stable for more than 2 months at room temperature. The new MDP is capable of producing G-1-P from maltodextrins, soluble starch, and glycogen with decreasing order of activity. The same glucans were accepted as primers in the direction of synthesis. Increasing pH values favoured the formation of G-1-P and optimized conditions for its production were established at a pH of 7.5. The maximum attainable yields of G-1-P by the action of MDP are limited by mainly two factors: (1) no more than approximately 20% of the initial inorganic phosphate could be converted into G-1-P and (2) the highest degrees of phosphorolytic maltodextrin degradation were in the range 30–35%. These values could be increased to more than 60% after pretreatment of the maltodextrins with pullulanase.
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  • 3
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background  The dogma in psoriasis is that due to pathogen-induced inflammatory responses, an autoreactive immune response is induced that leads to tissue destruction. However, this model might be too simplistic. Literature data suggest that the expression of enzymes crucial for fatty acid oxidation is upregulated in the skin of patients with psoriasis compared with healthy individuals.Objectives  To examine the influence of fatty acid oxidation on psoriasis with regard to expression and activity of the key enzyme in fatty acid oxidation, carnitine palmitoyltransferase-1 (CPT-1) and the effect of the CPT-1 inhibitor, Etomoxir.Methods  Experiments were performed with homogenates of lesional and healthy skin, fibroblast cultures and a model of human psoriatic skin transplanted on immune-deficient BNX mice.Results  CPT-1 was highly active in lesional skin. Etomoxir was able to block CPT-1 activity in skin, implying that this antagonist may have the potential to suppress psoriasis when administered topically. In the mouse model, Etomoxir had an antipsoriatic effect that was at least as good as that of betamethasone, as evidenced by reduction of epidermal thickness, keratinocyte proliferation and differentiation.Conclusions  We conclude that fatty acid metabolism and in particular CPT-1 may be an excellent target for treatment of psoriasis.
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  • 4
    ISSN: 1573-4919
    Keywords: alveolar macrophages ; tannin ; protein phosphorylation ; byssinosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Experiments were designed to determine if cotton bract tannin, a component of cotton mill dust, would promote the phosphorylation of alveolar macrophage proteins in doses potentially achievable in vivo. Rabbit alveolar macrophages were loaded with 32PO4 and challenged with various doses of tannin for time periods ranging from two seconds to 120 minutes. Changes in protein phosphorylation began after two seconds and were maximal at five to fifteen minutes. Dose response studies using an exposure time of one hour showed phosphorylation changes began at 1 µg/mL and were maximal at 10 to 30 µg/mL. Phosphorylation changes were similar to but not identical to those induced by the protein kinase C activator, phorbol myristate acetate (PMA). Calcium ionophore, A-23187 had no clear effect either alone or in conjunction with PMA. These results indicate that cotton bract tannin is able to rapidly promote protein phosphorylation of alveolar macrophages at doses potentially achievable in vivo. Other mechanisms in addition to those of protein kinase C appear to be involved in this protein phosphorylation process.
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  • 5
    ISSN: 1435-4373
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
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