Biomedical subjects
Publications and source records attributed to H P Zingsheim.
A statistical test based on a multiple comparison of Friedman's rank sums has been developed to determine the statistical significance of molecule projections obtained by non-crystallographic averaging techniques. The test, applied to electron microscope images of the acetylcholine receptor molecule, confirms the significance and quoted resolution of averages by Zingsheim et al. (1980, 1982a, b).
Sublimation rates of ice in the nitrogen-filled cryochamber of an ultramicrotome have been measured. The values are four to five orders of magnitude smaller than vacuum sublimation rates at the same temperature. This is a consequence of the much shorter mean free path length of water molecules in nitrogen at atmospheric pressure, as compared to freeze drying under vacuum. The partial pressure at the phase boundary and gas diffusion and convection determine the rate of freeze drying. This has implications for section handling and the design of transfer equipment. Generally, it means that the danger of even partial dehydration of semithick (0.5-1 micrometer) sections used mainly for X-ray microanalysis is less serious than commonly assumed.
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The removal of the 43 kDa peptide from postsynaptic membranes from the electric organ of Torpedo by alkaline treatment (pH 11) or by lithium diiodosalicylate at pH 8 results in similar ultrastructural changes that cannot be produced by the action of porcine pancreatic phospholipase A2 or lysophosphatidylcholine. Thin-layer chromatography fails to reveal significant alkaline hydrolysis of membrane lipids from postsynaptic membranes and erythrocyte ghosts under the conditions used for peptide extraction.
The acetylcholine receptor protein (AChR) from the electric organ of Torpedo marmorata is studied in its membrane-bound form by electron microscopy and single-particle image averaging. About half the molecule protrudes from the membrane surface by approximately 5 nm. The low-resolution 3-D structure of this hydrated portion, including its handedness, can be deduced from averaged axial and lateral projections and from freeze-etched membrane surfaces. In native membrane fragments, a dimeric form of the AChR is observed and the relative orientation of the AChR monomers within the dimer is established. The dimers disappear upon disulfide reduction of the membrane preparations, whereas the average axial projections of the AChR monomer remain unaffected. Since the existence of disulfide bonds linking AChR monomers between their respective delta-subunits is well documented, the approximate position of the delta-subunit within the low-resolution structure of the AChR molecule can be deduced from the structure of the dimers.
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A projection, at 15- to 20-A resolution, is presented of the structure of the membrane-bound acetylcholine receptor protein from Torpedo marmorata. The projection has its axis perpendicular to the membrane plane; its main contribution originates from a hydrated portion of the protein, which extends from the membrane into the aqueous medium. The structure is distinctly asymmetric, with individual morphological subunits barely resolvable. These results have been obtained by noncrystallographic averaging, using correlation functions, applied to electron micrographs of receptor-rich membrane fragments. The micrographs had been taken with minimal beam exposure in a scanning transmission electron microscope.
The influence of experimental conditions during rotary shadowing on the apparent particle size and the production of apparent holes or channels in the centre of a solid spherical particle are illustrated using ferritin.
Microtubules were reconstituted from homogeneous brain tubulin and homogeneous preparations of two different microtubule associated proteins, the high molecular weight MAP 2 proteins or the tau proteins. The resulting microtubules were characterized by three electron microscopical procedures: Thin sectional analysis of embeded material, negative staining analysis using a STEM microscope and high resolution metal-shadowing analysis. By all three procedures MAP 2 microtubules have a much rougher surface morphology than tau microtubules, in agreement with the much higher molecular weight of the MAP 2 proteins. Tau microtubules, however, do not show the very smooth surface of microtubules assembled from pure tubulin in the absence of any microtubule associated proteins. In the case of MAP 2 microtubules thin sectional analysis as well as metal shadowing reveals that the globular protrusions seen in negative staining analysis appear as linear side arms which may extend by as much as 30 nm on both sides from the microtubular wall proper, giving rise to an overall structure with a diameter close to 100 nm. The possible implication of such structures for in vivo situations is briefly discussed as is the possibility that the "halo-effect" around microtubules seen in vivo may be due to a structural organization similar to that of MAP 2 tubules in vitro.
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