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  • 11
    Electronic Resource
    Electronic Resource
    Identification of vacuolar serine proteinase as a major allergen of Aspergillus fumigatus by immunoblotting and N-terminal amino acid sequence analysis (2001)
    Oxford, UK : Blackwell Science, Ltd
    Clinical & experimental allergy 31 (2001), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Aspergillus species are common airborne fungi that have been identified as causative agents of extrinsic bronchial asthma. More than 10 allergens from A. fumigatus have been recently characterized by cDNA cloning.The objective of this study is to identify A. fumigatus allergens through immunoblot analysis using sera from asthmatic patients.IgE-binding components of A. fumigatus and IgE cross-reactivity among allergens of different prevalent airborne fungal species were analysed by immunoblot and immunoblot inhibition, respectively, using sera from asthmatic patients. The N-terminal amino acid sequences of major allergens identified were determined by Edman degradation.Among two batches (70 and 41 sera) of asthmatic sera tested, 19 (27%) and 14 (34%), respectively, have IgE immunoblot reactivity towards components of A. fumigatus. A 34-kDa protein that reacts with IgE antibodies in 15 (79%) and 11 (79%) of the 19 and 14 positive samples, respectively, may be considered a major allergen of A. fumigatus. The N-terminal amino acid sequences of the 34 kDa major allergen and the 30.5 and 30 kDa IgE-binding components of A. fumigatus showed sequence identity to that of the vacuolar serine proteinase from A. fumigatus. The results from immunoblot inhibition show IgE cross-reactivity among major allergens of A. fumigatus, P. notatum and P. oxalicum.Results obtained suggest that the 34 kDa major allergen of A. fumigatus may be a vacuolar serine proteinase. There is IgE cross-reactivity among serine proteinase allergens of A. fumigatus, P. notatum and P. oxalicum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2222.2001.01026.x
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  • 12
    Electronic Resource
    Electronic Resource
    Production and characterization of monoclonal antibodies to serine proteinase allergens in Penicillium and Aspergillus species (2000)
    Oxford BSL : Blackwell Science Ltd
    Clinical & experimental allergy 30 (2000), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Alkaline and/or vacuolar serine proteinases are major allergens in prevalent airborne Penicillium and Aspergillus species.〈section xml:id="abs1-2"〉〈title type="main"〉ObjectiveThe object of this study is to generate and characterize monoclonal antibodies against these serine proteinase allergens.〈section xml:id="abs1-3"〉〈title type="main"〉MethodsBALB/c mice were immunized individually with the Penicillium citrinum culture medium or the crude extract and culture medium preparations of Aspergillus fumigatus. Hybridoma cells that secrete monoclonal antibodies against serine proteinase allergens were selected by immunoblotting. Antigens in three different Penicillium (P. citrinum, P. notatum and P. oxalicum) and two different Aspergillus species (A. fumigatus, and A. flavus) recognized by these monoclonal antibodies were analysed by sodium dodecyl sulphate and two-dimensional polyacrylamide gel electrophoresis immunoblotting and N-terminal amino acid sequence analysis.〈section xml:id="abs1-4"〉〈title type="main"〉ResultsFour (PCM8, PCM10, PCM16 and PCM39) and one (FUM20) monoclonal antibodies against serine proteinase allergens were generated after fusion of NS-1 cells with spleen cells obtained from BALB/c mice immunized with antigens from P. citrinum and A. fumigatus, respectively. Immunoblotting results showed that PCM8 reacted with an alkaline serine proteinase allergen in P. citrinum and P. notatum. PCM10 and PCM39 reacted with the alkaline serine proteinase in two Penicillium (P. citrinum, P. notatum) and two Aspergillus species (A. fumigatus, and A. flavus) tested. PCM16 reacted with the alkaline serine proteinase allergen in P. citrinum, A. fumigatus and A. flavus but not with that in P. notatum. MoAb FUM20 reacted with the alkaline serine proteinase allergen in two Aspergillus species (A. fumigatus and A. flavus) but not with that in two different Penicillium species (P. citrinum, P. notatum) tested. Among these five monoclonal antibodies generated, only PCM39 and FUM20 can react with the vacuolar serine proteinase allergen in P. notatum, P. oxalicum and in A. fumigatus. The 35 kDa P. citrinum component that reacted with FUM20 has an N-terminal amino acid sequence of DSPSVEKNAP.〈section xml:id="abs1-5"〉〈title type="main"〉ConclusionFive monoclonal antibodies against different epitopes of the serine proteinase major allergens in prevalent Penicillium and Aspergillus species were generated in the present study. Antibodies obtained may be useful in the characterization and standardization of serine proteinase allergens in crude fungal extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2222.2000.00922.x
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  • 13
    Electronic Resource
    Electronic Resource
    APPLICATIONS OF GOAL PROGRAMMING IN ACCOUNTING (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of business finance & accounting 6 (1979), S. 0 
    Details
    ISSN: 1468-5957
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Economics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1468-5957.1979.tb01112.x
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  • 14
    Electronic Resource
    Electronic Resource
    Study of the \def\lambdabar{\ifvmode\noindent\fi{\hbox{$\lambda$}\kern-0.35em\raise0.7ex\hbox{-}\kern0.2em}}\lambdabar" phase in Zr–Nb alloys by Mössbauer and X-ray diffuse scattering (1975)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 8 (1975), S. 140-140 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The ω phase transformation in Zr–Nb alloys has been studied by measuring the X-ray diffuse scattering in the (110) plane and the Mössbauer diffuse scattering along the 〈111〉 direction of separate single crystals with compositions ranging from 8 to 30% Nb.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889875009867
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  • 15
    Electronic Resource
    Electronic Resource
    Ultrastructural and microanalytical aspects of developing osteodentin in rat incisors (1977)
    Springer
    Calcified tissue international 24 (1977), S. 215-222 
    Details
    ISSN: 1432-0827
    Keywords: Mineralization ; Osteodentin ; Intracellular ; Ultrastructure ; Microanalysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Newly formed osteodentin obtained from the anterior extremities of fetal or young rat incisors was observed by means of electron microscopy and electron probe X-ray microanalysis. Cells related to osteodentin formation frequently showed membrane bound intracellular bodies containing varying amounts of fine, needle-shaped crystals, which were identified as apatite. The intracellular clusters of apatite crystals were extruded from the cells through membrane fusion or cellular degeneration. These extracellular clusters seemed to be gradually incorporated into the mineralizing collagenous matrix, which developed around them. Frequent occurrence of dense, dotshaped or filamentous profiles suggested that the dense bodies seen in the perinuclear regions or in the Golgi area were the sites of crystal formation. Energy dispersive X-ray point analysis showed that the intracellular or extracellular apatite clusters contained sulfur in a concentration higher than was present in the mineralizing collagenous matrix. Furthermore, wave dispersive X-ray line analysis showed that the concentration of sulfur was higher in the osteodentin matrix than in the dentin matrix. The sulfur detected is presumed to be contained in acid mucopolysaccharides, which were distributed more heavily in the osteodentin matrix than in the dentin matrix. On the basis of these data, it was concluded that the unique chemical and structural characteristics of the osteodentin result primarily from the incorporation of apatite clusters of intracellular origin and associated acid mucopolysaccharides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02223319
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  • 16
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    DeCoster and Schafer, "Management Accounting: A Decision Emphasis", Second Edition (Book Review) (1979)
    Menasha, Wis. : Periodicals Archive Online (PAO)
    The Accounting Review. 54:4 (1979:Oct.) 845 
    Details
    ISSN: 0001-4826
    Topics: Economics
    Description / Table of Contents: BOOK REVIEWS, THOMAS J. BURNS, Editor
    Notes: Departments
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:5030-1979-054-04-000027
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  • 17
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    Multiple Objective Budgeting Models: A Simulation (1978)
    Menasha, Wis. : Periodicals Archive Online (PAO)
    The Accounting Review. 53:1 (1978:Jan.) 61 
    Details
    ISSN: 0001-4826
    Topics: Economics
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:5030-1978-053-01-000006
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  • 18
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    Wheelwright and Makridakis, "Forecasting Methods for Management", Second Edition (Book Review) (1978)
    Menasha, Wis. : Periodicals Archive Online (PAO)
    The Accounting Review. 53:2 (1978:Apr.) 593 
    Details
    ISSN: 0001-4826
    Topics: Economics
    Description / Table of Contents: BOOK REVIEWS, THOMAS J. BURNS, Editor
    Notes: Departments
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:5030-1978-053-02-000074
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  • 19
    Electronic Resource
    Electronic Resource
    Down-Regulation of Osteoblastic Cell Differentiation by Epidermal Growth Factor Receptor (2000)
    Springer
    Calcified tissue international 67 (2000), S. 141-150 
    Details
    ISSN: 1432-0827
    Keywords: Key words: Osteoblast — Differentiation — Epidermal growth factor receptor — Bone matrix.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract. The role of epidermal growth factor receptors (EGF-R) in osteogenic cell differentiation was investigated using preosteoblastic MC3T3-E1 (MC3T3) cells and osteoblast-like ROS 17/2.8 (ROS) cells. When cultured in the presence of β-glycerophosphate (GP) and ascorbic acid (AA), MC3T3 cells underwent spontaneous differentiation into osteoblasts which was confirmed as they expressed osteoblast markers such as alkaline phosphatase (ALP), bone sialoprotein (BSP) and osteocalcin (OC). Interestingly, the number of EGF-binding sites decreased during their differentiation into osteoblasts, and the osteogenic protein-1 (OP-1) treatment, which accelerated their differentiation, lowered the number of EGF-binding sites even further. On the other hand, ROS cells with high expression levels of osteoblast markers and no EGF-R, after being transfected with human EGF-R cDNA (EROS cells), expressed numerous EGF-binding sites as well as EGF-R mRNA and protein; in the process, they ceased to express osteoblast markers, indicating their dedifferentiation into osteoprogenitor cells. Both MC3T3 and EROS cells showed increased cell growth in response to EGF, whereas ROS cells did not. These results imply that the EGF/EGF-R system in osteogenic cells has a crucial function in osteoblast phenotype suppression and osteogenic cell proliferation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s00223001128
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  • 20
    Electronic Resource
    Electronic Resource
    Hyperprolinaemia in patients with deletion (22)(q11.2) syndrome (2000)
    Springer
    Journal of inherited metabolic disease 23 (2000), S. 847-848 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026773005303
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