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The genetic diversity of re-established population of endangered species Allium angulosum L. was tested as a one part of rescue program. Founder individuals were picked in Chropyně - Záříčí area (North Moravia, Czech Republic) and new population was set in Protected Landscape Area Litovelské Pomoravi (North Moravia, Czech Republic). The task was whether the newly founded population was made by representative individuals to cover (include) the genetic variability of source (mother) population. Items were tested with variability assay of six isozyme systems (G-6-PDH, AAT, PGM, EST, ACP, PGI) using discontinuous polyacrylamide gel electrophoresis (PAGE). The method stated relatively sufficient level of variability on condition that new population would be raised to prevent genetic changes. Application of more tests checking the genetic diversity within population could be useful during reintroduction and management of endangered plant species.
It was previously shown that the beta-spectrin ankyrin-binding domain binds lipid domains rich in PE in an ankyrin-dependent manner, and that its N-terminal sequence is crucial in interactions with phospholipids. In this study, the effect of the full-length ankyrin-binding domain of β-spectrin on natural erythrocyte and HeLa cell membranes was tested. It was found that, when encapsulated in resealed erythrocyte ghosts, the protein representing the full-length ankyrin-binding domain strongly affected the shape and barrier properties of the erythrocyte membrane, and induced partial spectrin release from the membrane, while truncated mutants had no effect. As found previously (Bok et al. Cell Biol. Int. 31 (2007) 1482–94), overexpression of the full-length GFP-tagged ankyrin-binding domain aggregated and induced aggregation of endogenous spectrin, but this was not the case with overexpression of proteins truncated at their N-terminus. Here, we show that the aggregation of spectrin was accompanied by the aggregation of integral membrane proteins that are known to be connected to spectrin via ankyrin, i.e. Na+K+ATP-ase, IP3 receptor protein and L1 CAM. By contrast, the morphology of the actin cytoskeleton remained unchanged and aggregation of cadherin E or N did not occur upon the overexpression of either full-length or truncated ankyrin-binding domain proteins. The obtained results indicate a substantial role of the lipid-binding part of the β-spectrin ankyrin-binding domain in the determination of the membrane and spectrin-based skeleton functional properties.
In most higher plants, the female gametophyte is deeply embedded in the ovule. In an earlier work we isolated egg cells from maize ovule tissues and analyzed egg cell lysates by polyacrylamide gel electrophoresis and mass spectrometry-based proteomics technology, and identified the major protein components expressed in these cells. The identified proteins included three cytosolic enzymes for the glycolytic pathway (glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, triosephosphate isomerase), two mitochondrial proteins (ATP synthase β-subunit and adenine nucleotide transporter), and annexin p35. Our data indicate that the plant egg cell is rich in an enzyme subset for energy metabolism. This article provides a short overview of major proteins in animal eggs, reports on major protein components of maize egg cells, and compares the major proteins between animal and plant eggs.
Sera obtained from patients with autoimmune liver disease were screened in indirect immunofluorescence microscopy for the presence of autoantibodies. Patients' sera, which strongly stained nuclei (ANA) with peripheral accentuation, were used for further experiments to define the corresponding antigen(s). Nuclei and nuclear subfractions were isolated from HeLaS3 cells and used as antigen source. Immunoblotting experiments were performed after separation of nuclear proteins by one- and two-dimensional polyacrylamide gel electrophoresis. Some ANA positive sera recognized the nuclear protein with molecular mass of approximately 200 kDa. Further analysis revealed that the patients' sera reacted with gp210, an integral protein of the nuclear pores. The incidence and clinical significance of these antibodies is discussed.
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