Isolation and characterization of human placenta fibronectin.

Abstract:

:Fibronectin was isolated from human placenta tissues and compared with human plasma fibronectin. Placenta and plasma fibronectins had similar amino acid compositions, immunological properties, and cell attachment-promoting activities, but differed in apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which could be accounted for at least partly by the difference in carbohydrate composition. Unlike plasma fibronectin, placenta fibronectin failed to form a precipitin line with concanavalin A in a double diffusion system. The non- or low-reactivity of placenta fibronectin with this lectin was also demonstrated by affinity chromatography with concanavalin A-agarose, in which more than 90% of the radiolabeled glycopeptides derived from placenta fibronectin was not retained on the gel. The two fibronectins also differed in the reactivity with Lens culinaris agglutinin of their glycopeptide fractions. These data indicate that placenta and plasma fibronectins are different in their carbohydrate structures and, therefore, suggest the presence of a tissue- or cell-specific mechanism for processing the carbohydrates of this glycoprotein.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Isemura M,Yamaguchi Y,Munakata H,Aikawa J,Kan M,Yamane I,Yosizawa Z

doi

10.1093/oxfordjournals.jbchem.a134808

subject

Has Abstract

pub_date

1984-07-01 00:00:00

pages

163-9

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

96

pub_type

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