Sea urchin coelomic fluid agglutinin mediates coelomocyte adhesion.
The sea urchin Paracentrotus lividus coelomic fluid was found to contain agglutinin which agglutinates animal erythrocytes and promotes adhesion of autologous coelomocytes. Hemagglutinating activity depended upon the presence of calcium ions and was relatively heat-stable. Through a combination of methods including ammonium sulfate precipitation and both size exclusion and ion exchange chromatographies, we purified the anti-rabbit agglutinating factor. The intact agglutinin migrates as a single band with an apparent M(r) of over 200,000. Three distinct protein bands with a calculated M(r) of 174,000, 137,000, and 76,000, respectively were observed under reducing conditions. The purified agglutinin strongly promoted the in vitro adhesion of autologous coelomocytes.
Canicattì
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Department of Biology, University of Lecce, Italy.
Pagliara
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Stabili
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L
D000373:Agglutinins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects*; D002449:Cell Aggregation / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000187:drug effects; D006801:Humans; D008970:Molecular Weight; D011817:Rabbits; D012617:Sea Urchins / Q000737:chemistry*; D014020:Tissue Extracts / Q000494:pharmacology
D000373:Agglutinins; D014020:Tissue Extracts