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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1981-8-20
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pubmed:abstractText |
The human kidney brush border membrane proteins were studied by crossed-immunoelectrophoresis. An antiserum against membrane vesicles was raised in rabbits and used in establishing a reference immunoelectrophoregram with the antigens released by Triton X-100. Among the precipitates observed, the following hydrolases were identified by zymogram staining: Microvillus aminopeptidase (EC 3..4.11.2), gamma-glutamyltransferase (EC 2.3.2.2), maltase (EC3.2.1.20) and trehalase (EC 3.2.1.28). Depletion of the antiserum with sealed, right-side-out vesicles was performed. No precipitates could be seen when the Triton X-100 extract was electrophoresed in a gel containing the depleted antibody. It is therefore suggested that the precipitation of membrane components by the complete antibody is mainly due to externally-located determinants and that the precipitates of the reference pattern correspond to membrane components pointing, at least in part, towards the tubular lumen. Evidence was also noted for a differential removal of antibodies directed against the different antigens. Such an observation could not be explained by the antigen accessibility nor by its amount in the membrane. Parallel crossed-immunoelectrophoresis of Triton X-100 and papain extracts gave rise to an "identity" pattern for only some antigens, particularly for microvillus aminopeptidase and maltase. It is thus strongly suggested that the papain-released form of these enzymes bears nearly all the antigenicity of the whole molecule.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:status |
MEDLINE
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pubmed:issn |
0300-9084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
375-87
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1981
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pubmed:articleTitle |
Crossed-immunoelectrophoretic study on human renal brush border membrane vesicles.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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