Isolation and characterization of rat plasma fibronectin

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Abstract
Rat plasma fibronectin was isolated and characterized and monospecific antibodies were prepared to it. Two components of fresh rat plasma (in the presence of proteinase inhibitors) bound to a gelatin-Sepharose affinity column. One protein was eluted with 4.0 M urea and was identified as fibronectin. Another protein was eluted from the gelatin-Sepharose column with 8.0 M urea and was identified as a 70,000 MW collagen-binding molecule. This 70,000 MW fragment was a normal constituent of blood plasma. Its presence did not represent a proteolytic degradation product formed during isolation. The antibodies prepared against rat fibronectin only weakly cross-reacted with plasma firbonectins of chicken, horse and human. These studies shed light on the metabolic interrelationships between fibronectin and other collagen-binding molecules.