Linked Life Data

2950930

Source:http://linkedlifedata.com/resource/pubmed/id/2950930

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-5-21
pubmed:abstractText
Brush-border membrane fractions were isolated from rat duodenum. Purity and integrity of the fraction was confirmed by electron microscopy, enzymic analysis and demonstration of Na+-dependent glucose uptake. The membranes were enriched 15-fold in alkaline phosphatase and alpha-glucosidase and 6-fold in HCO3--ATPase activities. Assays of latent activity indicated that these enzymes were predominantly localised to the external aspect of the microvillus membrane. The enzymes were solubilised and subjected to analysis by gel filtration, ion exchange and phenylboronate chromatography. No separation of alkaline phosphatase and HCO3--ATPase was obtained and it is suggested that they reflect the same enzyme activity. The apparent activation by HCO3- was investigated, and was found to be due to shifts in the pH dependency of the activity due to changes in ionic strength.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
924
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
159-66
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Studies on the localization and properties of rat duodenal HCO3--ATPase with special relation to alkaline phosphatase.
pubmed:publicationType
Journal Article