J. Biol. Chem., Vol. 259, Issue 2, 915-921, 01, 1984
Biochemical and immunochemical comparison of fibronectin and polynectin from porcine plasma
M Isemura, CC Hsu, Y Yamaguchi, H Munakata, Z Yosizawa, H Nagai, M Motomiya, M Kan and I Yamane
Polynectin, a glycoprotein of porcine blood plasma (also known as
glycine-rich gelatin-binding protein (Isemura, M., Sato, N., and Yosizawa,
Z. (1982) J. Biol. Chem. 257, 14854-14857] is similar to fibronectin with
respect to binding characteristics to affinity gels. However, no
immunoprecipitation reaction was observed either between polynectin and
anti-fibronectin antiserum, or between fibronectin and anti-polynectin
antiserum prepared in the present experiments. No cross- reaction was found
between fibronectin and polynectin by enzyme-linked immunosorbent assays.
Immunohistochemical studies revealed the presence in abundance of
polynectin in intestinal and gastric glands. It was found that the pattern
of distribution of polynectin was entirely different from that of
fibronectin. Polynectin, in contrast to fibronectin, exhibited no cell
attachment-promoting effects on BHK-21, a baby hamster kidney cell line,
and a cell line of human embryonic lung fibroblasts. In addition, changes
in binding characteristics to affinity gels after reduction and alkylation
differed between polynectin and fibronectin. Although both proteins appear
to have similar carbohydrate chains in view of the similar reactivities
with lectins, the results of the present experiments demonstrated that
polynectin is entirely different from fibronectin.
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