Reference

Biochemical and immunochemical comparison of fibronectin and polynectin from porcine plasma

Biochemical and immunochemical comparison of fibronectin and polynectin from porcine plasma. Isemura, Mamoru; Hsu, Cheng Chin; Yamaguchi, Yu; Munakata, Hiroshi; Yosizawa, Zensaku; Nagai, Hiromi; Motomiya, Masakichi; Kan, Mikio; Yamane, Isao (Sch. Med.In this study， 9005-49-6 and 74-79-3 are also used., Tohoku Univ., Sendai 980, Japan). J. Biol. Chem., 259(2), 915-21 (English) 1984. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Section cross-reference(s): 6 Polynectin, a glycoprotein of porcine blood plasma (also known as glycine-rich gelatin-binding protein), is similar to fibronectin with respect to binding characteristics to affinity gels. However, no immunopptn. reaction was obsd. either between polynectin and anti-fibronectin antiserum, or between fibronectin and antipolynectin antiserum. No cross-reaction was found between fibronectin and polynectin by ELISA. Immunohistochem. studies revealed the presence in abundance of polynectin in intestinal and gastric glands. 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 addn., changes in binding characteristics to affinity gels after redn. and alkylation differed between polynectin and fibronectin. Although both proteins appear to have similar carbohydrate chains, in view of the similar reactivities with lectins, polynectin is, apparently, entirely different from fibronectin. .

Factor VIII/von Willebrand factor has potent lectin activity

Factor VIII/von Willebrand factor has potent lectin activity. Booth, William J.; Furby, Fiona H.; Berndt, Michael C.; Castaldi, Peter A. (Dep. Med., Univ. Sydney, Westmead 2145, Australia). Biochem. Biophys. Res. Commun., 118(2), 495-501 (English) 1984. CODEN: BBRCA9. ISSN: 0006-291X. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Highly-purified plasma and platelet factor VIII/von Willebrane factor had potent lectin activity when measured in a hemagglutination assay. This lectin activity was inhibited by monoclonal and heterologous antibodies to factor VIII/von Willebrand factor as well as by hexosamines, mannose, and net-pos. 56-40-6 and 74-79-3 are just another two chemicals used in this study. charged amino acids. .