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Abstract
Fibronectin from human early pregnancy (5–8 weeks) placenta (epFN) has been isolated
by 2M urea-PBS extraction and purified by heparindashSepharose 4B affinity chromatography
followed by Sepha-rose CL-6B gel filtration, and compared with that of term placenta
(tpFN). According to the analysis on SDS-polyacrylamide gel electrophoresis (SDS-PAGE)
and Westerndashblots, epFN was similar to tpFN; both are composed of two 250 KD subunits,
larger than 220 KD subunits of plasma fibronectin (pFN). They reacted with antibodies
against pFN and monoclonal antibodies (mAbs) raised against three mainly functional
domains of amniotic fluid fibronectin (amFN), respectively.
However, the affinity of epFN with mAb against heparindashbinding domain was stronger
than that with mAb against gelatindashbinding domain; this phenomenon could not be
observed with tpFN and pFN. The results of lectindashbinding capacity indicated that
epFN was not only distinct from pFN but also from tpFN on its carbohydrate composition.
We also found there were much more Fndashbinding proteins in early placenta than in
term placenta. The significance of these results are discussed.
Keywords
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Article info
Publication history
Accepted:
November 15,
1993
Received:
June 4,
1993
Identification
Copyright
© 1994 Published by Elsevier Inc.
