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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Nutrient cycling in agroecosystems 16 (1988), S. 3-13 
    ISSN: 1573-0867
    Keywords: dicalcium orthosilicate ; calcium metasilicate ; mini-granulation ; extractable Si ; Si in saturation extract ; Oxisol ; Andept
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Silicate materials, dicalcium orthosilicate (Ca2SiO4), calcium metasilicate (CaSiO3), and mini-granulated CaSiO3, were incorporated into three highly weathered, low-Si soils. The mixtures were moistened to field moisture-holding capacity and incubated in plastic bags for 60 days at approximately 25°C, after which Si was extracted. Application rates of silicate materials were 0, 460, 920, and 1380 mg Si per kg soil. Two ranges of particles sizes, 0.25 to 0.84 mm and 0.074 to 0.15 mm CaSiO3 and Ca2SiO4 were compared. The soils were a Typic Gibbsiorthox, pH 4.6; a Humoxic Tropohumult, pH 4.2; and a Typic Hydrandept, pH 5.0. Materials were evaluated by four extraction procedures: shaking in water, water displacement from saturated soil, shaking in ammonium acetate solution, and biologically by roots of sugarcane (Saccharum Spp. hybrid). Silicate from the CaSiO3 materials were generally more readily extracted chemically and biologically than silicate from the Ca2SiO4. Solubility and availability of Si usually increased as primary particle size of the silicate materials decreased. The exceptions were associated with the most acid (pH 4.2) Ultisol. Mini-granulation did not reduce the effectiveness of CaSiO3 thus confirming agronomic feasibility of mini-granulation. Plant uptake of Si was most closely related to water-extractable soil Si, followed by Si in saturation extracts and then by NH4 OAc-extractable Si.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Plant and soil 81 (1984), S. 165-176 
    ISSN: 1573-5036
    Keywords: Avocado ; Ca ; Mn ; Oxisol ; P ; pH ; Phytophthora root rot ; Soil water
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary This experiment employed a factorial design combining 4 soil pH levels, 3 soil moisture levels, with and without the addition ofPhytophthora cinnamomi to the soil to evaluate the conditions that lead to Phytophthora root rot of avocado. An inverse relation between soil pH and leaf production (and root-weight) was observed in nondiseased plants. In soil infested withP. cinnamomi, plant growth and root weights were much depressed by low soil pH, and especially by low soil pH coupled with high soil moisture contents. These interactions were statistically highly significant. Root weights in pots withP. cinnamomi were closely related to the incidence of disease. A disease index was used to visually assess the conditions of roots. Isolation of the pathogen from diseased plant roots confirmed the accuracy of the disease index. A process of elimination suggsts that favorable soil Ca level and not high pHper se was responsible for disease suppression and that the devastating effects of low soil pH was produced by high Mn (and possibly Al) and associated low levels of Ca and P in soil solutions, which led to breakdown of biological control mechanisms.
    Type of Medium: Electronic Resource
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  • 3
    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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  • 4
    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
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  • 5
    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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  • 6
    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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