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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Nutrient cycling in agroecosystems 28 (1991), S. 95-101 
    ISSN: 1573-0867
    Keywords: Phosphate rock dissolution ; soil pH ; solution phosphorus ; phosphorus fractionation ; monocalcium phosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Soil Samples were collected from a field experiment conducted to evaluate the agronomic effectiveness of a reactive phosphate rock (PR), Sechura sand, relative to that of monocalcium phosphate (MCP) at different soil pHs and rates of application. The samples were analysed for P soluble in the soil solution and bicarbonate extractable P. The rate of dissolution of PR was calculated from the data on the fractionation of inorganic P. In MCP plots P in the soil solution decreased sharply with time especially at low pHs and high rates of fertiliser application. In PR plots the concentration remained with time at the same as or a slightly higher level than that was found one month after application. Solution concentration of P was lower at very high rates of PR application than at intermediate rates. In both MCP and PR plots bicarbonate extractable P decreased with increasing pH. Bicarbonate extractable P was linearly related to MCP but not to PR applied. The rate of dissolution and the proportion of PR dissolved decreased with increasing rates of PR application but the amount dissolved increased. Phosphate dissolved at high level of PR application did not seem to enhance proportionately either the concentration of P in soil solution or bicarbonate extractable P.
    Type of Medium: Electronic Resource
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  • 2
    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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  • 3
    ISSN: 1573-0867
    Keywords: Phosphate rock ; soil pH ; andepts ; white clover ; ryegrass ; soil phosphorus ; monocalcium phosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The agronomic effectiveness of an unground reactive phosphate rock from Sechura, Peru, was compared with that of monocalcium phosphate in a severely P deficient and highly P retentive soil (vitrandept) over a period of three years. Soil pHs were adjusted to pH 5.1, 5.3, 5.6 and 6.4. The sward consisted mostly of ryegrass (Lolium perenne) and white clover (Trifolium repens). Fertilisers were applied at six rates at pH 5.3 and three rates at other pHs in the first year. For two of the rates fertilisers were reapplied in the second year. Dry matter yields, P uptake and ground cover of clover were determined during the experimental period. In phosphate rock treated plots a negative linear relationship was obtained between soil pH and the logarithm of yield. The agronomic effectiveness of phosphate rock relative to monocalcium phosphate increased with time at all pHs. Calculated at fertiliser rates which produced near maximum yields, relative agronomic effectiveness at soil pHs 5.1, 5.3, 5.6 and 6.4 were respectively 58, 60, 18, and 5 in year one; 118, 125, 77 and 38 in year three. At pH 5.3, as the rate of application increased the relative agronomic effectiveness of the phosphate rock generally decreased in year one but was enhanced in the intermediate rates in years two and three. The data for ground cover of clover gave a similar trend to that for herbage yield and P uptake.
    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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