Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1981-8-20
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
375-87
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Crossed-immunoelectrophoretic study on human renal brush border membrane vesicles.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't