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  • 1
    Electronic Resource
    Electronic Resource
    Leucaena leucocephala seedling response to vesicular-arbuscular mycorrhizal inoculation in soils with varying levels of inherent mycorrhizal effectiveness (1989)
    Springer
    Biology and fertility of soils 8 (1989), S. 111-115 
    Details
    ISSN: 1432-0789
    Keywords: Glomus aggregatum ; Leucaena leucocephala ; Pinnule ; P status ; Tropical soils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary The symbiotic effectiveness of vesicular-arbuscular mycorrhizal (VAM) fungi present in widely differring tropical soils was evaluated in a greenhouse experiment. Small volumes of field soil, a standard inoculum (Glomus aggregatum) or both were introduced into a fumigated sand-soil medium amended with nutrients for optimum VAM activity. Leucaena leucocephala (Lam.) de Wit var. K8 was grown in the medium as an indicator plant. VAM effectiveness was monitored as a function of time by determining the P status of pinnules. The soils differed from each other with respect to the time their endophytes required for the expression of initial and maximum effectiveness and in the level of maximum effectiveness they exhibited. The effect of mycorrhizal inoculation, calculated as the ratio of the areas enclosed by the effectiveness curve of G. aggregatum to that enclosed by the effectiveness curves of test soils, was found to be a good indicator of the response of L. leucocephala to inoculation of soils with G. aggregatum
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00257753
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  • 2
    Electronic Resource
    Electronic Resource
    Separation of β-d-galactosidases in rabbit tissues: Genetics of neutral β-d-galactosidase (1983)
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00000016
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  • 3
    Electronic Resource
    Electronic Resource
    Genetics of a tissue esterase polymorphism (Est-6) in the rabbit (Oryctolagus cuniculus) (1987)
    Springer
    Biochemical genetics 25 (1987), S. 335-344 
    Details
    ISSN: 1573-4927
    Keywords: esterase ; genetics ; homology ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Genetic analysis of a polymorphic tissue esterase revealed a new locus (Est-6) with two alleles (Est-6 a andEst-6 b) on linkage group VI of the rabbit.Est-6 is closely linked to theEst-1,2,4 cluster. Esterase ofEst-6 is found in many organs, particularly in liver and small intestine, but not in erythrocytes and serum.Est-6 esterase hydrolyzes α-naphthyl acetate and butyrate, naphthol AS-D acetate, indoxyl acetate, and butyrate as well as 5-bromoindoxyl acetate,N-acetyl-l-alanine-α-naphthyl ester but not 4-methylumbelliferyl acetate and fluorescein diacetate. The enzyme is inhibited by bis-p-nitrophenyl phosphate and eserine but not byp-chloromercuribenzoate. It was classified as a carboxylesterase (EC 3.1.1.1). Based on chromosomal localization, tissue distribution, substrate specificity, inhibitor sensitivity, and range ofpI's, rabbitEst-6 is assumed to be homologous with mouseEs-7.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554543
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Separation of β-d-galactosidases in rabbit tissues: Genetics of neutral β-d-galactosidase (1983)
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02395402
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Genetics of two tissue esterase polymorphisms (Est-4 and Est-5) in the rabbit (1983)
    Springer
    Biochemical genetics 21 (1983), S. 773-780 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00498923
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Effectiveness of VAM fungi in nonsterile soils before and after optimization of P in soil solution (1993)
    Springer
    Plant and soil 151 (1993), S. 219-226 
    Details
    ISSN: 1573-5036
    Keywords: Glomus aggregatum ; indigenous ; Leucaena leucocephala ; propagules ; tropical soils ; VAMF inoculation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Five tropical soils were either not inoculated or inoculated with the vesicular-arbuscular mycorrhizal (VAM) fungus Glomus aggregatum. The degree to which VAM effectiveness was expressed in the soils was evaluated prior and after solution P status was adjusted for optimal VAM activity. VAM effectiveness determined by monitoring P concentrations of pinnules of Leucaena leucocephala leaves as a function of time and as dry matter yield determined at the time of harvest, indicated that in three of the soils VAM effectiveness was either very restricted or altogether unexpressed irrespective of vesicular-arbuscular mycorrhizal fungal (VAMF) inoculation if soil solution P was not optimized for VAM effectiveness. After P optimization, effectiveness was significantly increased by VAMF inoculation although in four of the soils, densities of indigenous VAMF propagules greatly exceeded that attained by the inoculum after it was mixed with soil. Mycorrhizal fungal inoculation effects varied from soil to soil, depending on the extent to which the effectiveness of indigenous and introduced endophytes was enhanced by P optimization and the similarity of inherent soil solution P concentrations to the range known to be optimum for VAM effectiveness. Of the indicator variables monitored, VAMF colonization was least sensitive to treatment effects followed by shoot P concentration measured at the time of harvest.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00016287
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    Paper (German National Licenses)
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