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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 38 (1982), S. 1942-1952 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 2
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    Wiesbaden : Periodicals Archive Online (PAO)
    Geographische Zeitschrift. 36:10 (1930) 635 
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Pediatric radiology 14 (1984), S. 332-334 
    ISSN: 1432-1998
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Rare earth filters are known to reduce radiation dose in radiological investigations. The present investigation used Er and Sm filters that were selected because of their chemical stability and ability to withstand prolonged exposure to the atmosphere. They were used in a comparison with a conventional aluminium filter in a range of paediatric radiological procedures. Introduction of the filters instead of the conventional filter, resulted in a dose reduction of up to twofold with no discernible deterioration in image quality.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    ISSN: 1573-4927
    Keywords: β-d-galactosidase ; β-d-glucosidase ; electrophoresis ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three different types of β-d-galactosidase (EC 3.2.1.23) could be distinguished in rabbit tissues using electrophoretic procedures. (1) Acid β-d-galactosidase with a low mobility and maximal activity at pH 3–5 was found in the particulate fraction of various tissue homogenates. This enzyme hydrolyzed 4-methylumbelliferyl-d-galactoside, but no activity against other glycoside substrates could be demonstrated. The enzyme was inhibited by galactono-(1 → 4)-lactone. (2) Lactose-hydrolyzing β-d-galactosidase with an intermediate mobility was found only in juvenile small intestine. Most of the activity was found in the particulate fraction of the cell. The enzyme hydrolyzed several other synthetic glycoside substrates besides lactose. It was most active at pH 5–6 and strongly inhibited by glucono-(1 → 5)-lactone but not much affected by galactono-(1 → 4)-lactone. (3) Neutral β-d-galactosidase with a fast mobility and maximal activity at pH 6–8 was found in the soluble fraction of homogenates from liver, kidney, and small intestine. This enzyme also showed a broad substrate specificity; it possessed activity against aryl-β-d-glucoside, -fucoside, and -galactoside substrates but not against lactose. The enzyme was strongly inhibited by glucono-(1 → 5)-lactone and (less) by galactone-(1 → 4)-lactone. Neutral β-d-galactosidase and neutral β-d-glucosidase (EC 3.2.1.21) are probably identical enzymes in the rabbit. Individual variation, in both electrophoretic mobility and activity, was found for neutral β-d-galactosidase. Genetic analysis of the electrophoretic variants revealed that two alleles at an autosomal locus are responsible for this variation.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 21 (1983), S. 773-780 
    ISSN: 1573-4927
    Keywords: esterase ; polymorphisms ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two polymorphic esterase systems were found after electrophoresis of rabbit tissue homogenates. Each of these systems is controlled by an autosomal locus with two alleles. Est-4 determines the absence (Est-4a) or presence (Est-4b) of two bands of esterase activity with intermediate anodal mobility and broad substrate specificity. This polymorphism was found to be present in liver, small intestine, and spleen but not in kidney, heart, and testis. Est-5 is coding for cathodally migrating esterases which differ in mobility (Est-5a and Est-5b). This polymorphism was found only in kidney and testis homogenates. Est-5 esterases are more active against α-naphthyl acetate than against β-naphthyl acetate and have no activity against α-naphthyl butyrate. Linkage analysis indicated that Est-4 is localized on rabbit LG VI as part of a cluster of esterase loci, whereas Est-5 segregates independently. Rabbits from two inbred and nine partly inbred strains were tested for these polymorphisms.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    ISSN: 1573-4927
    Keywords: β-d-galactosidase ; β-d-glucosidase ; electrophoresis ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three different types of β-d-galactosidase (EC 3.2.1.23) could be distinguished in rabbit tissues using electrophoretic procedures. (1) Acid β-d-galactosidase with a low mobility and maximal activity atpH 3–5 was found in the particulate fraction of various tissue homogenates. This enzyme hydrolyzed 4-methylumbelliferyl-d-galactoside, but no activity against other glycoside substrates could be demonstrated. The enzyme was inhibited by galactono-(1 → 4)-lactone. (2) Lactose-hydrolyzing β-d-galactosidase with an intermediate mobility was found only in juvenile small intestine. Most of the activity was found in the particulate fraction of the cell. The enzyme hydrolyzed several other synthetic glycoside substrates besides lactose. It was most active atpH 5–6 and strongly inhibited by glucono-(1 → 5)-lactone but not much affected by galactono-(1 → 4)-lactone. (3) Neutral β-d-galactosidase with a fast mobility and maximal activity atpH 6–8 was found in the soluble fraction of homogenates from liver, kidney, and small intestine. This enzyme also showed a broad substrate specificity; it possessed activity against aryl-β-d-glucoside, -fucoside, and -galactoside substrates but not against lactose. The enzyme was strongly inhibited by glucono-(1 → 5)-lactone and (less) by galactone-(1 → 4)-lactone. Neutral β-d-galactosidase and neutral β-d-glucosidase (EC 3.2.1.21) are probably identical enzymes in the rabbit. Individual variation, in both electrophoretic mobility and activity, was found for neutral β-d-galactosidase. Genetic analysis of the electrophoretic variants revealed that two alleles at an autosomal locus are responsible for this variation.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of inherited metabolic disease 6 (1983), S. 163-166 
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The concentration of taurine in the aqueous humour and serum of 21 rabbits with hereditary buphthalmia (Bu rabbits-genotypebu/bu) was compared with the aqueous and serum taurine levels of eight strain-related normal rabits (JAX) and nine non-strain-related normal rabbits (MCV). There was a significant difference in the mean aqueous taurine concentration in each of the three groups. The Bu rabbits had only 29% of the MCV rabbits' level while the JAX rabbits were intermediate with 56% of the MCV level. It is suggested that some of the JAX rabbits may be heterozygous and the Bu rabbits homozygous for a semi-dominant allele of a gene that is less efficient in taurine transport in the ciliary epithelium than the normal allele represented by the MCV animals.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-1335
    Keywords: Inbred rabbits ; Herpesvirus saimiri ; Malignant lymphoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Four young strain III/J rabbits of both sexes were inoculated with a single dose of prototype partially purified Herpesvirus saimiri (HVS) via IV and IM routes. All inoculated animals had enlarged lymph nodes, and significant levels of antibodies to HVS early, late, and membrane antigens were detectable during the infection. The animals died or were killed and HVS was isolated from the peripheral blood mononuclear cells and the various lymph nodes but not from the kidney. Microscopic examination showed that these animals had poorly differentiated lymphomas. The response of mononuclear cells to PHA from peripheral blood of infected animals showed depressed cell mediated immune responses. Humoral and cellular immunity responses during tumorigenesis were comparable to those reported in nonhuman primates with HVS-induced tumors. Thus, the inbred strain III/J appears to be an inexpensve suitable model for studies of oncogenic herpesvirus-induced cancers.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 94 (1933), S. 215-215 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Plant and soil 64 (1982), S. 331-341 
    ISSN: 1573-5036
    Keywords: Humic substances ; Molecular weight distribution ; N availability index ; Ninhydrindetectable N ; Relative N uptake ; Soil proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary Two soil extracts used for chemical indexes for N availability, 0.01M NaHCO3 and boiling 0.01M CaCl2, were analyzed in effort to learn more about the nature of the extracted organic matter (O.M.). The two extracts appeared to remove different fractions of the soil O.M. A study of five soils showed that the C/N value of the NaHCO3 extract (following decarbonation) was significantly higher than that of the total soil O.M.; while the C/N value in the boiling CaCl2 extract was not significantly different from that in the soil O.M. There was also significant variation in C/N values among soils for the boiling CaCl2 extract. The extracts of three soils were analyzed for apparent molecular weight distribution using gel filtration and the results compared to those for base-extracted humic substances. Almost all the molecules in the extracts had apparent molecular weights less than 21,000 daltons while 21 to 47% of the humic substances from the same soils (extracted with 0.5M NaOH) had molecular weights greater than 21,000 daltons. In the boiling CaCl2 extract, 78 to 87% of the humic substances had apparent molecular weights less than 1,000 daltons, whereas with the NaHCO3 extract, 42 to 83% of the humic substances were in the 1,000 to 21,000 dalton range. Forty-three to 92% of the N extracted by the NaHCO3 was in protein form, and 8 to 30% was ninhydrin-detectable. In the boiling CaCl2 extract 25 to 30% of the extracted N was ninhydrin-detectable. For the same 10 soils, ninhydrin-detectable N values of the boiling CaCl2 extract appeared closely related to greenhouse and field relative N uptake, while the ninhydrin-detectable N values of the NaHCO3 extract appeared unrelated to both. The protein N and protein in plus ninhydrin-detectable N values of the NaHCO3 extract were closely related to greenhouse relative N uptake only. The results of this study indicated that specific fractions of the soil O.M. were being extracted by the two solutions and that significant differences existed in the chemical nature of the two extracts.
    Type of Medium: Electronic Resource
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