Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity.
PD Yurchenco, EC Tsilibary, AS Charonis… - Journal of Biological …, 1985 - ASBMB
Laminin, a major structural glycoprotein of basement membranes, has been found to self-
associate in vitro into large polymers. The formation of these complexes can be followed by
the development of turbidity upon incubation in neutral phosphate buffer at 21-35 degrees C
and is seen to be time-, concentration-, and temperature-dependent. The process is
thermally reversible at 4 degrees C and the protein can be cycled between a dispersed and
an aggregated state by alternating between 4 and 35 degrees C. Following incubation at 35 …
associate in vitro into large polymers. The formation of these complexes can be followed by
the development of turbidity upon incubation in neutral phosphate buffer at 21-35 degrees C
and is seen to be time-, concentration-, and temperature-dependent. The process is
thermally reversible at 4 degrees C and the protein can be cycled between a dispersed and
an aggregated state by alternating between 4 and 35 degrees C. Following incubation at 35 …