Linked Life Data

10090333

Source:http://linkedlifedata.com/resource/pubmed/id/10090333

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-5-20
pubmed:abstractText
Carbonic anhydrase (CA) cytoplasmic isozymes CA I and CA II were found in human erythrocyte membrane ghosts, when prepared at pH 5.4 and pH 7.4, but not in ghosts prepared at pH 8.2. These findings could indicate that previously reported CA activity of ghosts was owing to contamination by CA I and CA II during the preparation of the ghosts. However, using a sensitive micro-assay, CA activity was also found in ghosts prepared at pH 8.2. This activity constitutes 0.2% of the erythrocytes' total CA-activity, and originates from a membrane-associated isoform of CA, located at the exterior membrane surface. It has immunochemical and kinetic properties like those of the membrane-bound CA IV, previously isolated from kidney, lung and small blood vessels. Its function is possibly to interact with the red cell membrane anionic transport protein, band 3, for the bicarbonate/chloride exchange.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0001-6772
pubmed:author
pubmed:issnType
Print
pubmed:volume
165
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Carbonic anhydrase IV activity is localized on the exterior surface of human erythrocytes.
pubmed:affiliation
Department of Medical Pharmacology, University of Uppsala, Biomedical Center, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't