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The anatomical structure and the distribution of arabinogalactan proteins were investigated in the ovule of an energetic plant Sida hermaphrodita (L.) Rusby after pollination. Material was collected from an experimental field of the University of Life Sciences in Lublin (Felin). After embedding for immunoflurescence, semi-thin sections were stained with toluidine blue or incubated with JIM 13 or MAC 207 monoclonal antibodies for immunolabeling of arabinogalactan proteins. The structure of the ovule showed some differences in comparison to other representatives of the Malvaceae family. Conversely, the distribution of arabinogalactan proteins did not differ significantly from their distribution in the ovules of other angiosperms at the investigated stage of development.
The microstructure of fresh and three days-stored Balady bread was studied using two different microscopic methods (LM and SEM). These both techniques revealed a great differences in the starch micro- structure as well as protein distribution between two layers of fresh Balady bread. The lower layer of Balady bread is characterized by the greater extent of starch geletinization as compared to the upper one. The upper layer of Balady bread is formed by continuos protein matrix with embedded lenticular-shaped starch granules. The microstructure of Balady bread after 3 days of baking differs from that of the fresh one mainly in the starch granules structure. The visible differences seem to be connected with different degree of starch gelatinization in each of the layers as well as free water (released from granules) redistribution between the layers. It was found that mainly these changes in stored bread allowed rapid rétrogradation of the main soluble starch component - amylose.
 Despite the emerging evidence suggesting a proatherogenic role of C-reactive protein (CRP) in atherosclerosis, the contribution of CRP in pathogenesis of atherosclerosis and atherothrombosis has not been unequivocally defined. The role of CRP in pathophysiology/pathology seems to largely depend on its structure. Two CRP isoforms, the native pentameric and the modified monomeric one, differ substantially in their physiological functions, which is thought to origin from the considerable structural heterogeneity of the CRP molecule. The present review provides an overview of the experimental evidence with relevance to the clinical role(s) of various CRP isoforms. The biological role of the protein, its structure and distribution are discussed with particular emphasis on the diverse properties of the pentameric and monomeric forms of CRP. Some methodological aspects, related to experimental models and techniques of CRP preparation, are also critically reviewed.
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