Identification of fibronectin and laminin in glycoprotein extracts of human aorta.

Glycoproteins were extracted from human atherosclerotic lesions by a phosphate buffered heparin solution and by 0.15 M NaCl, followed by sequential digestion of the tissue by collagenase and elastase. Proteins obtained from the extracts by fractional precipitation by (NH4)2SO4 at 40%, 60% and 100% saturation of the salt at pH 4.0 were analyzed for total protein and for fibronectin and laminin by immunodiffusion. Greater amounts of proteins were extracted from atherosclerotic lesions than from uninvolved tissue. The buffered heparin solution extracted several-fold more protein than 0.15 M NaCl. Fibronectin was found in most protein fractions from every extract, but the presence of laminin was noted only in the protein fractions precipitated at 40% saturation of (NH4)2SO4 in the extracts of the tissue by heparin.