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41.
The CAM has been tested in six species of the Aeonium genus by studying the diurnal fluctuation of organic acids, pH and night fixation of CO2. The existence of a mesophyll structure able to support this metabolism has been shown as well as a congruent periodicity in the pool of cell starch. We have calculated the S, ES and Sm indices in the six species. A series of regression equations of different grades and types were calculated and shown to have correlation coefficients statistically significant. This allows us to confirm the suitability of the Sm index as a rapid test to establish the CAM as postulated by former authors.  相似文献   
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In pregnant rats significant interstitial fluid pressure changes could be detected by means of capsules chronically implanted into the subcutaneous tissue. The capsular pressure increased significantly from a control value of -4.3 +/- 0.5 mmHg to -0.7 +/- 0.5 mmHg during the first period of pregnancy. Immediately before parturition the capsular pressure returned to the control level. During lactation the pressure rose as high as + 0.5 +/- 0.9 mmHg. After lactation the pressure returned again to the control value. By determining the extracellular fluid and plasma volume, as well as protein concentration in plasma and capsular fluid, the hydrostatic and colloid osmotic forces operating in the extracellular space could be analysed. It has been concluded that the observed capsular pressure changes during pregnancy are not solely of volumetric or colloid osmotic origin.  相似文献   
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A. Angel 《CMAJ》1974,110(5):540-548
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Data on porotic hyperostosis (usually from thalassemia or sicklemia) and on morphology as related to differential survival and fertility in Early Neolithic Nea Nikomedeia (N over 90) and Middle Bronze Age Lerna (N = 234) show (a) the importance of disease, mainly falciparum malaria, in determining fertility, (b) the irregular fit between prediction from fertile family groups and observed prehistoric microevolutionary change in Greece, (c) the probable effects of nutrition and disease.  相似文献   
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The importance of plasma HDL apolipoprotein concentration as a predictor of atherosclerotic risk is well recognized, yet the processes of HDL modification and degradation in various cells are not clearly understood. We examined the characteristics of HDL1 apolipoprotein degradation and cellular uptake by rat adipocytes and determined the effects of fasting on these processes. Epididymal and perirenal adipocytes were isolated from male Wistar rats (310 +/- 4 g) fed ad libidum and incubated with 5 micrograms of rat 125I-labeled HDL1 (d: 1.07-1.10 g/mL) mL-1 for 2 h at 37 degrees C. Cellular uptake of HDL1 was calculated as the trichloroacetic acid precipitable radioactivity associated with adipocytes following incubation. Intracellular and medium degradation of HDL1 were determined as trichloroacetic acid soluble 125I counts associated with cells and measured in the postincubation medium, respectively. Fifty to sixty percent of cellular uptake and degradation of HDL1 was inhibited by the addition of 25-fold excess unlabeled HDL. HDL1 degradation measured in the medium was 10- to 12-fold greater than cellular uptake of HDL1 apolipoproteins. Intracellular degradation of HDL1 was negligible. The presence of EDTA in the incubation medium reduced HDL1 degradation measured in the medium, but enhanced HDL1 cellular uptake. Conditioned medium separated from cells after 2 h of incubation at 37 degrees C in the absence of HDL and subsequently incubated with 125I-labeled HDL1 for an additional 2 h at 37 degrees C, degraded less than 5% of HDL compared with degradation in the presence of cells. These results suggest that rat adipocytes degrade, or modify, HDL1 particles, possibly by interactions with cell surface proteases.(ABSTRACT TRUNCATED AT 250 WORDS)  相似文献   
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Summary Production of extracellular hydrogen peroxide by fungal oxidases is been investigated as a requirement for lignin degradation. Aryl-alcohol oxidase activity is described in extracellular liquid and mycelium ofPleurotus eryngii and studied under non-limiting nitrogen conditions. This aryl-alcohol oxidase catalyses conversion of primary aromatic alcohols to the corresponding aldehydes and H2O2, showing no activity with aliphatic and secondary aromatic alcohols. The enzyme is stable at pH 4.0–9.0, has maximal activity at 45°–50°C and pH 6.0–6.5, is inhibited by Ag+, Pb2+ and NaN3, and has aK m of 1.2 mM using veratryl alcohol as substrate. A single protein band with aryl-alcohol oxidase activity was found in zymograms of extracellular and intracellular crude enzyme preparations fromP. eryngii.  相似文献   
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