These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Dynamic, temperature-sensitive association of 125-i-nerve growth factor in vitro with ganglionic and non-ganglionic cells from embryonic chick.
    Author: Norr SC, Varon S.
    Journal: Neurobiology; 1975 May; 5(2):101-18. PubMed ID: 1134617.
    Abstract:
    125-I-NGF was found to associate with embryonic chick dorsal root ganglia (DRG) through two processes. A time-saturable process included the binding of NGF to surface receptors with an apparent affinity constant in the range of 10(-7)M minus 1 and at a level of 4 f moles/mug tissue protein. The second process was time-linear, temperature-sensitive, and included both bound and non-competable NGF. While metabolic inhibitors had little effect, histone and insulin considerably increased the uptake. A comparison of 125-I-NGF and 125-I-peroxidase uptake suggested that the time-linear uptake of 125-I-NGF must include only bound NGF and incubation medium. Sequestration of the proteins taken up was indicated by the lack of release of radiolabeled material at 4 degrees C, even in the presence of native proteins. All these characteristics are consistent with an interpretation that DRG cells can take up NGF and other proteins by a pinocytotic process. Similar NGF binding and uptake properties were found to occur in cells from a variety of other embryonic chick tissues.
    [Abstract] [Full Text] [Related] [New Search]