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. 2008 Nov 27;60(1):197–212. doi: 10.1093/jxb/ern280

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© 2008 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 4. — Presence of 175 kDa myosin in isolated phragmoplasts. (A) Immunoblotting of isolated phragmoplasts was carried out using antibody against actin (b), tubulin (c), 175 kDa (d), or 170 kDa myosin heavy chain (e). Actin, tubulin, and the 175 kDa myosin, but not 170 kDa myosin, were present in the isolated phragmoplasts. (a) CBB-stained 8% SDS–polyacrylamide gel. The molecular masses of standard proteins are indicated on the left in kilodaltons. (B) Double immunofluorescence staining of isolated phragmoplasts with the antibody against 175 kDa myosin heavy chain (a and d) and RP (b and e). The 175 kDa myosin (a) was concentrated at the boundary between the opposite actin filament bundles (arrow in b) in the isolated phragmoplast. (c) Merged image of a and b. In the view from the pole, the 175 kDa myosin (d) was co-localized with the actin filament ring of the isolated phragmoplast (e). The bar represents 20 μm.