Linked Life Data

28905

Source:http://linkedlifedata.com/resource/pubmed/id/28905

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1978-11-18
pubmed:abstractText
Brush border (BB) membranes, isolated from human kidney cortex by density gradient centrifugation, revealed a distinct pattern of structural proteins as could be shown by bio- and immunochemical studies. Marker enzymes such as gamma-glutamyltranspeptidase (GGTP) and alanine-aminopeptidase (AAP) were characterized as extrinsic; alkaline phosphatase (AP) was characterized as an integral constituent of the BB membrane. The surface of the BB membranes exhibited numerous 5 nm particles bound through a linear component to the peripheral BB matrix (negative staining). Increase of AAP and GGTP (30%) activity in the supernatant after proteolytic treatment of BB fragments paralleled selective release of these constituents from the membranes. The surface components were found to be part of BB concanavalin A and wheat germ agglutinin receptor sites. Labelled antisera directed against surface glycoprotein fractions gave a specific immuno fluorescence staining of only the luminal plasma-membrane from the proximal tubule epithelia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-1725
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
85-95
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Biochemical, immunological and ultrastructural studies on brush-border membranes of human kidney.
pubmed:publicationType
Journal Article