Properties of the Specific Binding of 125I-Nerve Growth Factor to Responsive Peripheral Neurons
Year: 1974
Type: article
Abstract: The interaction of nerve growth factor (NGF) with its receptor(s) on the surface membranes of responsive chick embryo sympathetic and sensory neurons has been examined using 1251-NGF prepared by a solid phase iodination technique.The specific binding of lz51-NGF to both types of neurons is a complex process.It is nonsaturable at concentrations of i*51-NGF as high as lo-* M and displays apparent multiple affinities (KA Z lOlo to lo6 liters per mole).The specific binding is rapid (kl = 7.5 X 106 M-' s-l at 24') and reversible (kel = 3.8 x lo-' s-l at 24").Native NGF at a concentration of 2 x 10m7 M accelerates the dissociation of bound lz51-NGF 30.fold at 24" (native NGF k-* = 1.2 x 10F2 s-i), suggesting that the apparent multiple affinities for the binding of 1251-NGF are due to a negatively cooperative interaction of NGF receptors.Insulin, at a concentration of 2 x 10m7 M, inhibits the specific binding of 1251-NGF 15 to 20%.Lower or higher concentrations of insulin were not as effective.The material specifically binding '251-NGF comigrates with the surface membrane label iz51-cu-bungarotoxin in two subcellular fractionation procedures.The total amount of specific binding material and the binding per microgram of tissue protein vary during embryonic development in a manner reflecting the temporal pattern of biological responsiveness of sympathetic and dorsal root ganglia.
Source: Journal of Biological Chemistry
Institution: Washington University in St. Louis
Language: English
Subfield: Cellular and Molecular Neuroscience
Field: Neuroscience
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1480084963