Publications by authors named "Ververgaert P"

It is argued that the different modes of fracturing of the erythrocyte membrane and the outer membrane of Escherichia coli with respect to the intramembraneous particles have their definite biochemical and structural counterpart i.e.,.

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1. The influence of Ca2+ on the polymorphic phase behaviour of cardiolipin has been investigated employing 31P NMR and freeze-fracture techniques. The close correlation between the results obtained here and previous X-ray studies (Rand, R.

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Freeze-fracture electron microscopy demonstrates that in photosynthetic membranes of the blue-green alga Anacystis nidulans quenched from a temperature below growth temperature, areas devoid of membrane particles occur. We suggest that this phenomenon is related to phase transitions in the photosynthetic membrane.

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The size and population density of large and small particles from freeze-fractured chloroplasts of three wild-type algae and of normal spinach were determined. Computer analyses of low-temperature absorption spectra of chloroplast preparations from these species were performed, and a possible correlation between the occurrence of seven chlorophyll complexes and the aforementioned properties of the intramembranous particles was studies. It was found that only single-sized particles occur in a species containing neither chlorophyll b nor chlorophyll a-685 complexes.

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During cell division in the Xenopus egg (diameter 1.25 mm) new cell membrane is formed in the furrow region (rate of growth approx 4-10(4) mum2/min). Freeze-fracture electron microscopy has produced the following data.

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Adhesion followed by fusion of LP-X vesicles with the erythrocyte membrane is an important contribution to the erythrocyte enlargement in patients with intra or extra hepatic cholestasis. Adhesion of LP-X vesicles is demonstrated by thin section and freeze-etch electronmicroscopy. Fusion of LP-X with the erythrocyte membrane is deduced from biochemical data and freeze-etch electronmicroscopy in that the uptake of cholesterol and lecithin coincides with the increase in smooth areas on the fracture faces of the erythrocyte membrane.

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Freeze etching showed that the loss of each of the major outer membrane proteins b, c or d in mutants of Escherichia coki K12 does not influence the morphology of fracture faces of the outer membrane. Mutants that possess a heptose-deficient lipopolysaccharide and which in addition are deficient in one or more major outer membrane proteins exhibit a reduction in the number of intramembranous particles of the outer membrane. Moreover it was shown that lipid phase transitions induce a lateral lipid protein separation in the outer membrane, similar to that found in the cytoplasmic membrane.

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As a basis for physicochemical studies on the membranes of the strictly anaerobic bacteria Veillonella parvula, Anaerovibrio lipolytica, and Megasphaera elsdenii, the fatty acyl and alk-1-enyl moieties on the phosphoglycerides of these organism were characterized. Uncommon is the high proportion of a heptadecenoic acyl and alk-1-enyl moiety in these three lactate-fermenting bacteria. In contrast to V.

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Calorimetric experiments showed a marked effect of Ca2+ and Mg2+ on the thermotropic behaviour of dimyristoyl phosphatidylglycerol. 2. Concentrations of Ca2+ and Mg2+ lower than 1 ion to 2 molecules of phosphatidylglycerol produced a shift of the phase transition to higher temperatures and an increase in the enthalpy change which is consistent with a closer packing of the lipid molecules in the liposomes.

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Protoporphyrin causes a photodynamic damage of the red blood cell membrane. After illumination of red blood cells in the presence of protoporphyrin three effects can be observed: 1. Red blood cell membranes show particle aggregation on the outer and inner fracture face, as seen in freeze-etch electron microscopy.

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In the presence of Mg2+ ions phosphatidylglycerol shows supercooling which leads to the formation of a metastable gel phase. This contrasts with the behaviour of this negatively charged phospholipid in the presence of Ca2+ ions (Biochim. Biophys.

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