Co-staining with DAPI and CellMaskTM green using fluorescence microscope imaging revealed accumulation of hypericin in cell membranes of Caco-2 cells

A vertebrate disk membrane is composed of 40 % lipids and 60 % proteins. Its fracture faces have been classed into the plasmic (PF) and exoplasmic faces (EF), complementary with each other, like those of most other types of cell membranes. The hypothesis assuming the PF particles as representing membrane-associated proteins has been challenged by serious questions if they in fact emerge from the crystalline formation or decoration effects during freezing and shadowing processes. This problem seems to be yet unanswered, despite the remarkable case of the purple membrane of Halobacterium, partly because most observations have been made on the replicas from a single face of specimen, and partly because, in the case of photoreceptor membranes, the conformation of a rhodopsin and its relatives remains yet uncertain. The former defect seems to be partially fulfilled with complementary replica methods.

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Introduction to Cell Membranes at Molecular Resolution

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100070217 ◽

1978 ◽

Vol 36 (3) ◽

pp. 497-502

Author(s):

R.J. Barrnett

Keyword(s):

Cell Membranes ◽

International Federation ◽

Mountain Range ◽

Cellular Membranes ◽

Short History ◽

Biological Organization ◽

Macromolecular Assemblies ◽

The Past

This subject, is like observing the panorama of a mountain range, magnificent towering peaks, but it doesn't take much duration of observation to recognize that they are still in the process of formation. The mountains consist of approaches, materials and methods and the rocky substance of information has accumulated to such a degree that I find myself concentrating on the foothills in the foreground in order to keep up with the advance; the edifices behind form a wonderous, substantive background. It's a short history for such an accumulation and much of it has been moved by the members of the societies that make up this International Federation. My panel of speakers are here to provide what we hope is an interesting scientific fare, based on the fact that there is a continuum of biological organization from biochemical molecules through macromolecular assemblies and cellular membranes to the cell itself. Indeed, this fact explains the whole range of towering peaks that have emerged progressively during the past 25 years.

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Scanning x-ray fluorescence microscopy and principal component analysis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100133394 ◽

1992 ◽

Vol 50 (2) ◽

pp. 1752-1753

Author(s):

Brian Cross

Keyword(s):

Principal Component Analysis ◽

Fluorescence Microscopy ◽

Spatial Resolution ◽

High Speed ◽

Image Acquisition ◽

Principal Component ◽

Fluorescence Microscope ◽

Acquisition Rate ◽

X Ray ◽

Speed Up

A relatively new entry, in the field of microscopy, is the Scanning X-Ray Fluorescence Microscope (SXRFM). Using this type of instrument (e.g. Kevex Omicron X-ray Microprobe), one can obtain multiple elemental x-ray images, from the analysis of materials which show heterogeneity. The SXRFM obtains images by collimating an x-ray beam (e.g. 100 μm diameter), and then scanning the sample with a high-speed x-y stage. To speed up the image acquisition, data is acquired "on-the-fly" by slew-scanning the stage along the x-axis, like a TV or SEM scan. To reduce the overhead from "fly-back," the images can be acquired by bi-directional scanning of the x-axis. This results in very little overhead with the re-positioning of the sample stage. The image acquisition rate is dominated by the x-ray acquisition rate. Therefore, the total x-ray image acquisition rate, using the SXRFM, is very comparable to an SEM. Although the x-ray spatial resolution of the SXRFM is worse than an SEM (say 100 vs. 2 μm), there are several other advantages.

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