Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-4-26
pubmed:abstractText
The kinetic parameters involved in determining the steady-state interaction of Multi-CSF with FDCP-1 cells at 37 degrees C have been determined by kinetic analysis under steady-state conditions and by curve-fitting the rate of approach to steady-state conditions. The two methods are in substantial agreement and yield values of Vr = 28 receptors/cell/min for the rate of appearance of receptors at the cell surface, ke and kt = 0.061 min-1 and 0.0044 min-1 for the rate constants of internalization of occupied and unoccupied receptors, respectively, kh = 0.008 min-1 for the rate constant of degradation of internalized ligand, ka = 2.9 X 10(8) M-1 min-1 for the rate constant of association and kd = 0.11 min-1 for the rate constant of dissociation of ligand with receptor. Analysis of steady-state conditions indicated that Multi-CSF caused substantial down-regulation of surface receptors and that considerably more Multi-CSF was inside the cell than at the cell surface. The implications of these results for utilization rates of Multi-CSF by FDCP-1 cells and the relationship of receptor occupancy to biological activity are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0897-7194
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-39
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Binding, internalization, and degradation of 125I-multipotential colony-stimulating factor (interleukin-3) by FDCP-1 cells.
pubmed:affiliation
Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria, Australia.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't