. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. CARBOHYDRATES OF B. GLABRATA 237. Figure 2. Isoelectrical focusing of the extracted water-soluble or- ganic matrix fraction of the Biomphalaria glahrata shell and application of lectins. Std = standard proteins; Coom = matrix, stained with Coo- massie brilliant blue; ConA. WGA. and MPA = lectins: Alz = matrix, stained with alcian blue. the belt. The calcium cells in the interstitiiim bound al- most all lectins, but no inhibition by the specific sugars occurred, indicating merely an unspecitic reaction. Discussion Chit in The
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. CARBOHYDRATES OF B. GLABRATA 237. Figure 2. Isoelectrical focusing of the extracted water-soluble or- ganic matrix fraction of the Biomphalaria glahrata shell and application of lectins. Std = standard proteins; Coom = matrix, stained with Coo- massie brilliant blue; ConA. WGA. and MPA = lectins: Alz = matrix, stained with alcian blue. the belt. The calcium cells in the interstitiiim bound al- most all lectins, but no inhibition by the specific sugars occurred, indicating merely an unspecitic reaction. Discussion Chit in The hexosamines of the IM were mainly alkali-resis- tant, so the matrix could contain chitin. The infrared spec- trometry could not, however, confirm this assumption (Fig. lb). Bielefeld cl al. (1993a), using electron micros- copy, found WGA binding sites in the periostracum of B. glabrata. After a chitinase digestion, the reactivity of these sites was reduced, but not negative. The cells at the PG and the belt, however, were not affected by chitinase. The results indicate that chitin is one of the GlcNac- positive components of the periostracum of B. iilaivaia. but the amount may be considered rather low. Glycoproteins und proteoglycans Prominent among the proteins of the SM of B. glahrata is one that has a size of kDa and an point of A'-terminal microsequencing revealed that 15 or 16 of the 24 amino acids identified in the protein were hydrophobic (Marxen and Becker. 1997). Because of its high pi, this protein cannot be directly involved in the binding of calcium. As demonstrated by the binding of lectins to the lEF gel (Fig. 2, Table IV), this protein is glycosylated with glucosyl and mannosyl moieties, singly or in combination. Thus, this glycopro- tein contains hydrophobic as well as hydrophilic domains and may have evolved from a membrane protein. In the SM of MytUiis I'dulis. Keith cl al. (1993) found a protein with a size of 21 kDa and a h
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