Dimeric character of fibronectin, a major cell surface-associated glycoprotein
J Keski-Oja, DF Mosher, A Vaheri - Biochemical and Biophysical Research …, 1977 - Elsevier
J Keski-Oja, DF Mosher, A Vaheri
Biochemical and Biophysical Research Communications, 1977•ElsevierExposed proteins of cultured chick and human fibroblasts were labeled by lactoperoxidase-
catalyzed iodination and analyzed by polyacrylamide gel electrophoresis in sodium dodecyl
sulfate. Extracts from both cell types contained the characteristic, heavily labeled band of
fibronectin (molecular weight= 2.2× 10 5) when analyzed after reduction with 2-
mercaptoethanol. Without prior reduction, however, the 2.2× 10 5 molecular weight band
was missing and replaced by labeled bands of 4.4× 10 5 and of very high molecular weight …
catalyzed iodination and analyzed by polyacrylamide gel electrophoresis in sodium dodecyl
sulfate. Extracts from both cell types contained the characteristic, heavily labeled band of
fibronectin (molecular weight= 2.2× 10 5) when analyzed after reduction with 2-
mercaptoethanol. Without prior reduction, however, the 2.2× 10 5 molecular weight band
was missing and replaced by labeled bands of 4.4× 10 5 and of very high molecular weight …
Abstract
Exposed proteins of cultured chick and human fibroblasts were labeled by lactoperoxidase-catalyzed iodination and analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Extracts from both cell types contained the characteristic, heavily labeled band of fibronectin (molecular weight = 2.2 × 105) when analyzed after reduction with 2-mercaptoethanol. Without prior reduction, however, the 2.2×105 molecular weight band was missing and replaced by labeled bands of 4.4×105 and of very high molecular weight. This finding indicates that fibroblast cell-surface fibronectin, like the fibronectin purified from plasma, is composed of two high molecular weight polypeptides hed together by disulfide bonds, and suggests that the dimer may in addition form disulfide-bonded multimers.
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