Abstract
Laminin is a noncollagenous glycoprotein (Mr ≈ 106) localized specifically in basement membranes. In vertebrates it consists of disulfide-linked polypeptide chains of Mr ≈ 200′000 (B1- and B2-chain) and Mr ≈ 400′000 (A-chain). By electron microscopy it is visualized as an asymmetric cross with one long and three short arms each bearing terminal globules (cf Paulsson 1987). By extraction with a physiological buffer containing a metal ion chelator (EDTA) laminin copurifies with nidogen (Mr ≈ 150′000) which is bound near the middle of one of the short arms (Paulsson et al 1987). To investigate structural variations of laminin during evolution we applied this extraction protocol to some invertebrates covering the main groups of phylogeny: we have chosen sea urchins belonging to the deuterostomia, leeches as an example for the protostomia and anthomedusae for the radiata.
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References
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© 1989 Springer-Verlag Berlin Heidelberg
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Beck, K., McCarthy, R.A., Chiquet, M., Masuda-Nakagawa , L., Schlage, W.K. (1989). Structure of the Basement Membrane Protein Laminin: Variations on a Theme. In: Aebi, U., Engel, J. (eds) Cytoskeletal and Extracellular Proteins. Springer Series in Biophysics, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73925-5_19
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DOI: https://doi.org/10.1007/978-3-642-73925-5_19
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-73927-9
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