Polypeptides of human plasma fibronectin are similar but not identical.

Human plasma fibronectin migrated in electrophoresis after reduction of the disulfide bonds in SDS-polyacrylamide gels as two closely spaced polypeptide bands. These polypeptides, the A chain (Mr 220 000) and the B chain (215 000), were isolated from slices of slab gels. The two isolated chains were immumologically indistinguishable when tested by double immunodiffusion against antiserum to plasma fibronectin. Identical peptides were obtained from both chains after Staphylococcus aureus proteinase digesting or after cyanogen bromide cleavage, respectively. Kinetic analysis of plasmin digestion of isolated dimeric fibronectin, however, suggested that the A chain was cleaved more rapidly than the B chain and that the primary plasmin cleavage products of fibronectin, the 200 000 and 190 000 polypeptides, were derived from the A and B chain, respectively. The basis for the difference between the A and B chains of human plasma fibronectin identified here, is, at present, unknown. Proteolytic or some other posttranslational processing of a common fibronectin polypeptide seems unlikely since also the newly synthesized fibronectin, isolated from human fibroblast cultures pulse-labeled for 5 min, appeared as two closely spaced polypeptide bands in SDS-gel electrophoresis.