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The paper presents results from the comparative studies upon methods of industrial fodder mixtures homogeneity evaluation. Competence of participating laboratories to make a legal control within that issue was confirmed. Achieved results on the mixing level (variability coefficient) of fodder mixtures for turkeys and swine were lower than 10% – limit value. Reproducibility limits of results achieved by two laboratories determining chlorides and calcium within legal control were set for 5% (chlorides) and 3% (calcium). Acceptance of expanded uncertainty at the same level as uncertainty of analytical methods was recommended.
In most studies of nest-site selection the data of habitat parameters are treated with analysis of variance. A basic assumption of this test is the homogeneity of variance. Here, we show that the nest-site selection process leads to lower variance of the selected parameters than in the case of random points which generally describe the available average characteristics of the environment. Thus, the variance should be accounted for in studies on nest-site selection and it should be treated not as a problem (as it is usually done), but as a source of additional important information on the selection process. Comparison only of mean values often does not lead to significant differences between nest site parameters and random points which may result from a small effect size (when animals select features similar to the general mean of available characteristics). Deeper insight into variance of the site parameters may elicit important results. We illustrate this issue with real data on nest site (islets and shores of water reservoirs) selection in the Common Gull Larus canus. Four (islet’s area, vegetation height on islets, vegetation cover on shore and distance to nearest shrub or tree on shore) from eight parameters were favored by the birds and, as predicted, their variance values were lower than of those not selected (vegetation cover on islets, distance of the islets to shoreline, vegetation height on shore and distance to water).
This paper presents the results of granulometric analyses of sawdust of unmodified and thermally- modified ash wood (Fraxinus exelsior L.) sawed on a narrow-kerf sash gang saw. The sawdust of dry thermally-modified ash produced in the sawing process on a frame sawing machine PRW15-M at a feed speed in the range of 0.36-1.67 m·min-1 has chip granularity ranging from 33.5 μm to 9.9 mm; whereas unmodified ash wood sawdust consists of chips in a granularity range from 35.6 μm to 13.8 mm. It was observed that thermally-modified ash sawdust is finer, with a distinctly larger share of the fraction in the granularity range a = 125-500 μm and a slightly increased share of the fraction in the range a = 32-125 μm. Changes in mechanical characteristics of modified wood were also observed in the technological usefulness of a part of dry sawdust chip in the granularity range a = 250 μm-2.4 mm. While the homogenous share of chips in sawdust produced in the process of sawing of dry ash wood was HSCha = 81-84 %, the demonstrated homogenous share of chips in ash sawdust formed in the process of sawing of dry thermally-modified wood was lower by 4-6 %.
Adenosine 5'-phosphoramidate (NH2-pA) is an uncommon natural nucleotide of poorly understood biochemistry and function. We studied a plant enzyme potentially involved in the catabolism of NH2-pA. A fast and simple method comprising extraction of yellow lupin (Lupinus luteus) seed-meal with a low ionic strength buffer, ammonium sulfate and acetone fractionations, removal of contaminating proteins by heat denaturation, and affinity chromatography on AMP-agarose, yielded homogenous nucleoside 5'-phosphoramidase. Mass spectrometric analysis showed that the lupin hydrolase exhibits closest similarity to Arabidopsis thaliana Hint1 protein. The substrate specificity of the lupin enzyme, in particular its ability to split the P-S bond in adenosine 5'-phosphorothioate, is typical of known Hint1 proteins. Adenosine 5'-phosphofluoride and various derivatives of guanosine 5'-phosphoramidate were also substrates. Neither common divalent metal cations nor 10 mM EDTA or EGTA affected the hydrolysis of NH2-pA. The enzyme functions as a homodimer (2 × 15 800 Da). At the optimum pH of 7.0, the Km for NH2-pA was 0.5 µM and kcat 0.8 s-1 (per monomer active site). The properties of the lupin nucleoside 5'-phosphoramidase are compared with those of its counterparts from other organisms.
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