Purification of an antibody‐like protein from the sea star Asterias rubens (L.)

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Abstract

Cells from sea star Asterias rubens axial organs stimulated with trinitrophenyl (TNP) or fluoresceinyl‐haptened polyacrylamide beads and subsequently stimulated in vitro with the same antigen produced and released a specific antibody‐like protein which induced lysis of haptened sheep erythrocytes in the presence of serum complement. The anti‐TNP antibody‐like protein isolated by ammonium sulfate precipitation, gel filtration and affinity chromatography exhibited a single precipiting peak after crossed immunoelectrophoresis against rabbit antiserum to partially purified culture supernatant. The anti‐TNP antibody‐like protein gave a specific affinity precipitate in crossed affino‐electrophoresis using a p‐nitrobenzoyl‐substituted gel. The analysis by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis under both reducing and nonreducing conditions evidenced a unique 30‐kDa polypeptide chain. According to gel filtration experiments, the molecular weight of the major component isolated by affinity chromatography was about four times higher. Therefore, the antibody‐like molecule could be a tetrameric protein devoid of any disulfide bond. Copyright © 1986 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim

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Delmotte, F., Brillouet, C., Leclerc, M., Luquet, G., & Kader, J. ‐C. (1986). Purification of an antibody‐like protein from the sea star Asterias rubens (L.). European Journal of Immunology, 16(11), 1325–1330. https://doi.org/10.1002/eji.1830161103

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