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  • Articles: DFG German National Licenses  (3)
  • 2000-2004  (3)
  • 2003  (3)
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  • Articles: DFG German National Licenses  (3)
Material
Years
  • 2000-2004  (3)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Successful induction of immune tolerance in a patient with haemophilia B with inhibitor (2003)
    Oxford, UK : Blackwell Science Ltd
    Haemophilia 9 (2003), S. 0 
    Details
    ISSN: 1365-2516
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We describe successful induction of immune tolerance (IT) in a 10-month-old boy with severe haemophilia B. Urticaria developed soon after starting prophylactic treatment and was associated with an inhibitor at 7 Bethesda units mL−1. Initially, we tried low dose factor IX therapy to induce IT with only a transient effect. The patient experienced an intracranial haemorrhage. A simple bolus dose of FIX eradicated the inhibitor. Thereafter he has been free from inhibitor and nephrotic syndrome for more than 5 years, although he receives FIX three times a week.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2516.2003.00754.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Polyphenol Oxidase from Bean Sprouts (Glycine max L.) (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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: : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb14107.x
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Morphological and biochemical studies of human β-mannosidosis: identification of a novel β-mannosidase gene mutation (2003)
    Oxford, UK : Blackwell Science Ltd
    British journal of dermatology 149 (2003), S. 0 
    Details
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary Background There are seven well-known lysosomal storage diseases that produce angiokeratoma corporis diffusum clinically. β-Mannosidosis (MANB1; OMIM248510), first reported in humans in 1986, is a rare hereditary lysosomal storage disease caused by a deficiency of the enzyme β-mannosidase. Since then, 13 cases of β-mannosidase deficiency in ten families have been described. A human β-mannosidase mutation has been reported only by Alkhayat et al. in 1998. Objectives To clarify its pathogenesis we did electron microscopic, biochemical and molecular biological investigations of a Japanese patient with β-mannosidosis. Methods Ultrastructural analyses, enzyme assays, cell culture and mRNA and genomic DNA were sequenced to find mutations in the β-mannosidase gene. Results Electron microscopy of skin biopsy specimens from the patient showed cytoplasmic vacuolation of lysosomes in blood and lymph vessels, endothelial cells, fibroblasts, secretory portions of eccrine sweat glands, neural cells and basal keratinocytes in the epidermis. This vacuolation was also observed in cultured keratinocytes and fibroblasts. Assays of seven enzyme activities in plasma and cultured skin fibroblasts showed a marked decrease of β-mannosidase activity. Sequencing the β-mannosidase cDNA revealed a four-base (ATAA) insertion between exons 7 and 8, resulting in a frameshift at codon 321 and termination at codon 325. Analysis of the patient's genomic DNA revealed a novel homozygous A(+1)→G splice site mutation in intron 7. Conclusions To our knowledge, this is the first case of β-mannosidosis reported in Japan and the second report in which a gene mutation is identified. The biological importance of β-mannose moieties in glycoproteins in basal keratinocytes is suggested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2133.2003.05365.x
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    Paper (German National Licenses)
    Fulltext
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