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Figure 2 | BMC Plant Biology

Figure 2

From: Characterization of bacterial-type phosphoenolpyruvate carboxylase expressed in male gametophyte of higher plants

Figure 2

Specificities of the antibodies produced and immunoprecipitation. (A) An anti-AtBTPC antibody recognized an AtBTPC band of the expected size (ca. 116 kDa) in flower bud proteins from wild-type Arabidopsis (AFwt) and an LlBTPC band of equivalent size in the lily anther (LA) proteins. No AtBTPC band was detected in the flower bud proteins from the atppc4 mutant plants (AFppc4/ppc4). (B) The anti-AtPTPC antibody recognized an AtPTPC band of the expected size (ca. 110 kDa) in the flower bud proteins from wild-type Arabidopsis (AFwt) and an LlBTPC band of equivalent size in the lily anther (LA) proteins. Note that the anti-AtPTPC antibody recognized AtPPC1, AtPPC2, and AtPPC3 because of the high homology of their amino acid sequences (see Additional file 2). (C) Immunoprecipitation with FK2 of LlBTPC (upper) and LlPTPC (middle) from lily anthers containing late bicellular pollen. Mouse serum was used as the control. Note that FK2 immunoprecipitated greater amounts of LlPTPC (lower band) than did mouse serum. The upper bands detected with anti-AtPTPC antibody (asterisks) likely represent monoubiquitinated LlPTPC (Ub-LlPTPC). The proteins precipitated with FK2 were immunoblotted with a polyclonal antibody directed against Ub (αpoly-Ub), which detects both ubiquitinated protein and free Ub (bottom), confirming that FK2 precipitates Ub-related proteins.

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