Divalent cations in cerebral impedance and cell membrane morphology

1969 ◽  
Vol 23 (1) ◽  
pp. 29-50 ◽  
Author(s):  
W.R. Adey ◽  
B.G. Bystrom ◽  
A. Costin ◽  
R.T. Kado ◽  
T.J. Tarby
Keyword(s):  
Cell Membrane ◽  
Divalent Cations ◽  
Membrane Morphology

scholarly journals Receptor Binding Sites and Antigenic Epitopes on the Fiber Knob of Human Adenovirus Serotype 3

1998 ◽  
Vol 72 (11) ◽  
pp. 9121-9130 ◽  
Author(s):  
Herbert Liebermann ◽  
Renate Mentel ◽  
Ulrike Bauer ◽  
Patricia Pring-Åkerblom ◽  
Rudolf Dölling ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Cell Membrane ◽  
Receptor Binding ◽  
Binding Sites ◽  
Divalent Cations ◽  
Membrane Receptors ◽  
Enzyme Linked Immunosorbent Assay ◽  
Receptor Binding Site ◽  
Cell Membrane Proteins ◽  
Antigenic Epitopes

ABSTRACT The adenovirus fiber knob causes the first step in the interaction of adenovirus with cell membrane receptors. To obtain information on the receptor binding site(s), the interaction of labeled cell membrane proteins to synthetic peptides covering the adenovirus type 3 (Ad3) fiber knob was studied. Peptide P6 (amino acids [aa] 187 to 200), to a lesser extent P14 (aa 281 to 294), and probably P11 (aa 244 to 256) interacted specifically with cell membrane proteins, indicating that these peptides present cell receptor binding sites. Peptides P6, P11, and P14 span the D, G, and I β-strands of the R-sheet, respectively. The other reactive peptides, P2 (aa 142 to 156), P3 (aa 153 to 167), and P16 (aa 300 to 319), probably do not present real receptor binding sites. The binding to these six peptides was inhibited by Ad3 virion and was independent of divalent cations. We have also screened the antigenic epitopes on the knob with recombinant Ad3 fiber, recombinant Ad3 fiber knob, and Ad3 virion-specific antisera by enzyme-linked immunosorbent assay. The main antigenic epitopes were presented by P3, P6, P12 (aa 254 to 269), P14, and especially the C-terminal P16. Peptides P14 and P16 of the Ad3 fiber knob were able to inhibit Ad3 infection of cells.

Cell-Glass Separation Depends on Salt Concentration and Valency: Measurements on Dictyostelium Amoebae by Finite Aperture Interferometry

1982 ◽  
Vol 54 (1) ◽  
pp. 299-310
Author(s):  
DAVID GINGELL ◽  
SHEILA VINCE
Keyword(s):  
Ionic Strength ◽  
Cell Membrane ◽  
Divalent Cations ◽  
Optical Measurements ◽  
Surface Glycoprotein ◽  
Monovalent Cations ◽  
Cell Surface Glycoprotein ◽  
Cellular Slime ◽  
Finite Aperture ◽  
Interacting Surfaces

Using pre-aggregation amoebae of the cellular slime mould Dictyostelium discoideum we have investigated the influence of cation concentration and valency on cell-glass separation. For computing the separation we used interference reflection microscopy and converted measured image irradiance to distance by finite aperture theory. Alterations in ionic strength caused virtually instantaneous reversible changes in the interference image due to changes in cell membrane-glass separation. In solutions containing monovalent cations, a change in ionic strength from 20 mM to 0.5 mM increased the separation of the plasmalemma from the glass by 60 nm. Divalent cations were better than monovalent cations at maintaining a small separation. Our results show that both divalent and trivalent cations adsorb to one or both of the interacting surfaces, in addition to acting as electrostatic double-layer counterions. The optical measurements also show that the cell membrane-glass gap is not reduced to zero by counterion screening; this is apparently due to the presence of a cell surface glycoprotein coat.

Cell membrane morphology analysis using an infrared sensor system

2013 ◽  
Vol 179 ◽  
pp. 150-156 ◽  
Author(s):  
Sander van den Driesche ◽  
Filippo Iuliano ◽  
Christoph Haiden ◽  
Daniela Pucciarelli ◽  
Heimo Breiteneder ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Sensor System ◽  
Infrared Sensor ◽  
Membrane Morphology ◽  
Morphology Analysis

scholarly journals STRUCTURE AND STAINING CHARACTERISTICS OF MYOFIBER EXTERNAL LAMINA

1973 ◽  
Vol 21 (8) ◽  
pp. 703-714 ◽  
Author(s):  
S. I. ZACKS ◽  
M. F. SHEFF ◽  
A. SAITO
Keyword(s):  
Cell Membrane ◽  
Phosphotungstic Acid ◽  
Divalent Cations ◽  
Periodic Acid ◽  
Amorphous Layer ◽  
Ruthenium Red ◽  
Low Ph ◽  
Acid Solutions ◽  
Colloidal Iron ◽  
Periodic Acid Schiff

A variety of cytochemical methods were used to investigate the composition of mouse sarcolemma. We found that the sarcolemma is a complex composed of the myofiber cell membrane, a thin zone external to the cell membrane that contains groups that bind colloidal iron and thorium at low pH and a thicker amorphous layer that fails to stain with colloidal iron and thorium at low pH. The entire complex is periodic acid-Schiff-positive and stains with ruthenium red and strongly acid solutions of phosphotungstic acid. Although the specificity of these cytochemical stains is controversial, data obtained with them and from preliminary analyses of myofiber external lamina (EL) indicate that the myofiber cell coat is chiefly composed of glycoprotein containing a large number of carboxyl groups. The EL within the subneural apparatus of the neuromuscular junction differs from noninnervated areas in the fusion of Schwann cell and myofiber EL, the absence of collagen microfibrils, the more intense binding of divalent cations and the less intense stain with phosphotungstic acid in strongly acid solutions.

THE INHIBITION OF KETO ACID OXIDATION BY PYOCYANINE

1957 ◽  
Vol 3 (2) ◽  
pp. 313-318 ◽  
Author(s):  
J. J. R. Campbell ◽  
A. M. MacQuillan ◽  
B. A. Eagles ◽  
R. A. Smith
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Pseudomonas Fluorescens ◽  
Acid Level ◽  
Divalent Cations ◽  
Acid Oxidation ◽  
Keto Acid ◽  
Proteus Vulgaris ◽  
Whole Cells ◽  
Cell Extracts

When tested against Pseudomonas fluorescens, pyocyanine was found to stop the oxidation of a number of substrates at the keto acid level. This inhibition could be reversed by the addition of divalent cations. Of these, magnesium was most effective. The pigment was found to be similarly effective against the oxidations of Proteus vulgaris. Whole cells of Escherichia coli were not affected by the dye, whereas cell extracts were, indicating that the dye did not penetrate the cell membrane.

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