Download Egg Bioscience and Biotechnology by Yoshinori Mine PDF

By Yoshinori Mine

Constitution and chemical compositions of eggs -- Biosynthesis and structural meeting of eggshell elements -- Bioavailability and physiological functionality of eggshells and eggshell membranes -- Bioactive parts in egg white -- Bioactive parts in egg yolk -- Egg allergens -- construction of novel proteins in chicken's eggs -- Egg items and destiny views

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The amino acid sequence of ovocleidin-17 contains 142 amino acids, including two phosphorylated serines (Mann and Siedler 1999). Reyes-Grajeda et al. 5 Å resolution, and showed that it has a mixed α/β structure containing a single C-type lectin-like domain. CHEMICAL COMPOSITION OF EGGS 21 However, although OC17 shares the conserved scaffold of the C-type lectins, it does not bind carbohydrates. Daengprok et al. (2003) found that the total Ca transport across Caco-2 monolayers grown on a permeable support was increased 64% in the presence of soluble eggshell matrix proteins.

20 STRUCTURE AND CHEMICAL COMPOSITION OF EGGS 2000), ovotransferrin (Panheleux et al. 2000; Dominguez-Vera et al. 2000), clusterin (Mann et al. 2003), osteopontin (Fernandez et al. 2003; Lavelin et al. 2000), ovocleidin-17 (Reyes-Grajeda et al. 2002, 2004; Mann and Siedler 1999; Panheleux et al. 2000; Dominguez-Vera et al. 2000; Lakshminarayanan et al. 2005), ovocleidin-116 (Nimtz et al. 2004; Hincke et al. 1999; Dominguez-Vera et al. 2000), ovocalyxin-32 (Gautron et al. 2001; Dominguez-Vera et al.

1999) reported almost exact 222 symmetry in the crystal structures of the four avidin subunits. Each avidin chain, composed of 128 amino acid residues, is arranged in an eight-stranded antiparallel β-barrel, whose inner region defines the D-biotin binding site. A fairly rigid binding site, readily accessible in the apoprotein structure, is sterically complementary to the shape and polarity of biotin. Swamy et al. (1996) used Fourier transform infrared (FTIR) spectroscopy to study avidin secondary structure and complexation with biotin and biotin–lipid assemblies.

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