Abstract
Laminin is a large (Mr ∼ 800000) extracellular glycoprotein which is a ubiquitous component of basement membranes. It consists of three different polypeptide chains, A (Mr ∼ 400000), B1, and B2 (both Mr ∼ 200000) which are linked by disulphide bonds to form a characteristic asymmetric cross structure (Engel et al, 1981).
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References
Engel J, Odermatt E, Engel A, Madri J.A, Furthmayr H, Rohde H, and Timpl R (1981) Shapes, domain orgainisation and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. J Mol Biol 150: 97–120.
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© 1989 Springer-Verlag Berlin Heidelberg
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Hunter, I., Beck, K., Schulthess, T., Engel, J. (1989). Triple Coiled-Coil Regions of Laminin: Specificity and Chain Stability. 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_20
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DOI: https://doi.org/10.1007/978-3-642-73925-5_20
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