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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-7-21
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pubmed:abstractText |
Erythrocytes adhere to each other when suspended in supra-threshold concentrations of dextran of molecular mass of 40 kD or greater. The plasma membranes are parallel to each other over the entire length of the contact seam at the lower effective polymer concentrations. When cells are pretreated with the proteolytic enzyme pronase or the sialidase neuraminidase the membranes are not parallel but make contact at spatially periodic locations along the membrane surface. Pronase induced reduction of cell electrophoretic mobility rapidly reaches a limiting value. Nevertheless, prolonged pre-exposure to enzyme leads to a continuing reduction in contact separations. This result taken with the observation that, for equal loss of electrophoretic mobility, a shorter contact separation results from pronase rather than neuraminidase pre-treatment implies that a non-electrostatic consequence of pronase pre-treatment dominates membrane interaction in the experimental regimes examined here. The average lateral contact separation for different enzyme regimes lay in the range 3.3 microns to a limiting lower value of about 0.7 micron. There was a good correlation between the logarithm of a contact separation index (the approach of separation distance to its limiting value) against the logarithm of a derived index related to net attractive interaction for a wide range of experimental conditions. Treatments which increased attraction or decreased repulsion (e.g. increased dextrans concentration or enzyme pre-treatment) lead to shorter lateral contact separation. This result is qualitatively consistent with the predicted behaviour for the dominant wavelength arising from interfacial instability of a thin aqueous film between adjacent membranes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dextrans,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Pronase,
http://linkedlifedata.com/resource/pubmed/chemical/Sialic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Suspensions
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pubmed:status |
MEDLINE
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pubmed:issn |
0175-7571
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-62
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7685691-Cell Adhesion,
pubmed-meshheading:7685691-Cell Communication,
pubmed-meshheading:7685691-Cells, Cultured,
pubmed-meshheading:7685691-Dextrans,
pubmed-meshheading:7685691-Electrophoresis,
pubmed-meshheading:7685691-Erythrocytes,
pubmed-meshheading:7685691-Humans,
pubmed-meshheading:7685691-Kinetics,
pubmed-meshheading:7685691-Microscopy, Electron,
pubmed-meshheading:7685691-Models, Biological,
pubmed-meshheading:7685691-Molecular Weight,
pubmed-meshheading:7685691-Neuraminidase,
pubmed-meshheading:7685691-Osmolar Concentration,
pubmed-meshheading:7685691-Pronase,
pubmed-meshheading:7685691-Sialic Acids,
pubmed-meshheading:7685691-Solutions,
pubmed-meshheading:7685691-Suspensions
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pubmed:year |
1993
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pubmed:articleTitle |
Influence of polymer concentration and molecular weight and of enzymic glycocalyx modification on erythrocyte interaction in dextran solutions.
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pubmed:affiliation |
School of Pure and Applied Biology, University of Wales College of Cardiff, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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