[HTML][HTML] High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-ζ/β with tenascin-R, amphoterin, and the …
P Milev, A Chiba, M Häring, H Rauvala… - Journal of Biological …, 1998 - ASBMB
We have studied the interactions of the nervous tissue-specific chondroitin sulfate
proteoglycans neurocan and phosphacan with the extracellular matrix protein tenascin-R
and two heparin-binding proteins, amphoterin and the heparin-binding growth-associated
molecule (HB-GAM), using a radioligand binding assay. Both proteoglycans show saturable,
high affinity binding to tenascin-R with apparent dissociation constants in the 2–7 nmrange.
Binding is reversible, inhibited in the presence of unlabeled proteoglycan, and increased …
proteoglycans neurocan and phosphacan with the extracellular matrix protein tenascin-R
and two heparin-binding proteins, amphoterin and the heparin-binding growth-associated
molecule (HB-GAM), using a radioligand binding assay. Both proteoglycans show saturable,
high affinity binding to tenascin-R with apparent dissociation constants in the 2–7 nmrange.
Binding is reversible, inhibited in the presence of unlabeled proteoglycan, and increased …