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. 1998 Feb;116(2):733–742. doi: 10.1104/pp.116.2.733

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Specific binding of CWI to recombinant Nt-inh1 protein immobilized on a Ni-affinity column. A total cell wall protein fraction from tobacco cells was passed through a column packed with recombinant Nt-inh1 protein bound to the Ni-NTA matrix (Qiagen). After extensive washing the recombinant Nt-inh1 protein with bound CWI was eluted with EDTA buffer. A, Analysis by SDS-PAGE and Coomassie staining. Total cell wall protein (lane 1) was passed through Ni-NTA columns with bound Nt-inh1 protein (lanes 2–5) or without Nt-inh1 protein (lanes 6–9); lanes 2 and 6, flow-through; lanes 3 and 7, EDTA eluate; lanes 4 and 8, washing fractions before EDTA elution; lane M, marker proteins. B, Immunoblot analysis of the same fractions as in A developed with an antiserum directed against CWI. The 28-kD splitting product results from intrinsic CWI lability (Weil and Rausch, 1994).