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Comparison of the structures of human fibronectin and plasma cold-insoluble globulin

✍ Scribed by Balian, Gary ;Crouch, Ed ;Click, Eva Marie ;Carter, William G. ;Bornstein, Paul

Publisher: Wiley (John Wiley & Sons)
Year: 1979
Tongue: English
Weight: 713 KB
Volume: 12
Category: Article
ISSN: 0091-7419
DOI: 10.1002/jss.400120410

No coin nor oath required. For personal study only.

✦ Synopsis

Human amniotic fluid fibronectin and plasma fibronectin (cold-insoluble globulin) are indistinguishable both immunologically and by amino acid composition. Cyanogen bromide and tryptic peptides also suggest substantial structural homology. However, carbohydrate analysis has demonstrated additional saccharides in fibronectin and an overall increase in carbohydrate content relative t o coldinsoluble globulin. Furthermore, limited proteolytic cleavage of the two proteins indicates differences in primary structure or in conformation. Using affinity-purified antibodies t o cold-insoluble globulin, a glucosamine-labeled pronaseresistant component, probably proteoglycan, was found t o coprecipitate with fibronectin, suggesting an association between these two macromolecules in the connective tissue matrix.

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