Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-10-14
pubmed:abstractText
Nerve growth factor (NGF) binds to two specific receptors on sensory nerve cells. These two receptors are characterized by different equilibrium dissociation constants. The higher affinity (type I) receptors have an equilibrium dissociation constant of 3.3 X 10(-11) M. The lower affinity (type II) receptors have an equilibrium dissociation constant of 1.7 X 10(-9) M. These two receptors are not a result of negative cooperativity, but apparently are different receptors. At 22 degrees C the rate of association is 1 X 10(7) M-1 S-1 and the rates of dissociation are 6.5 X 10(-4) S-1 (type I) and 3.2 X 10(-2) S-1 (type II). After binding, a time-dependent process occurs that makes that NGF inaccessible to the external milieu (sequestered). The sequestration process is energy-dependent, but apparently temperature-independent. The data suggest that only the type I receptors are involved in the sequestration process. This process is similar to that observed on sympathetic neurons and may be the first step in the internalization of NGF by responsive cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
436-42
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Sequestration of 125I-labeled beta nerve growth factor by embryonic sensory neurons.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.