Linked Life Data

3999012

Source:http://linkedlifedata.com/resource/pubmed/id/3999012

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1985-7-11
pubmed:abstractText
alpha 1-Acid glycoprotein (AAG) exists in a variety of sialylated states which can be influenced by certain disease states. The purpose of the present study was to establish the effect of the sialylation state of AAG on the binding of a model cationic drug (propranolol). Extensive in vitro enzymatic desialylation of isolated human AAG was achieved utilizing neuraminidase bonded to agarose beads. Propranolol binding to native and desialylated AAG was determined by equilibrium dialysis. Desialylated AAG exhibited a modest increase in propranolol free fraction due to a decrease in the affinity constant (Ka) compared to untreated AAG (3.3 X 10(5) M-1 versus 4.0 X 10(5) M-1, respectively). A modest 15% increase was predicted for the free fraction of propranolol in serum containing desialylated AAG at therapeutic propranolol concentrations (less than 0.1 microgram/ml). Therefore, the clinical significance of desialylated AAG appears to be minor with respect to propranolol binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-3549
pubmed:author
pubmed:issnType
Print
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
473-5
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Effect of the sialylation state of alpha 1-acid glycoprotein on propranolol binding.
pubmed:publicationType
Journal Article