## Abstract Lectins of different binding specificity were used to analyze the oligosaccharide chains of the 220โ and 180โkD proteins of the __Unio elongatulus__ egg vitelline coat (vc). The lectins ConA and RCA~1~ reacted with both glycoproteins, and four other lectins reacted with one or other vc
Vitelline coat of Unio elongatulus: II. Biochemical properties of the 220- and 180-kD components
โ Scribed by R. Focarelli; A. Santucci; R. Lampariello; Dr. Floriana Rosati
- Book ID
- 102951621
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 570 KB
- Volume
- 40
- Category
- Article
- ISSN
- 1040-452X
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โฆ Synopsis
In a previous study we found that two glycoproteins with apparent molecular weights of 220 kD and 180 kD account for 80-90% of the material dissolved from the vitelline coat of the egg of the bivalve mollusk, Unio elongatulus (Focarelli and Rosati, 1993 Mol Reprod Dev 35:44-51). In this study we isolated and purified these glycoproteins by electroelution. The two proteins differ in many respects: the 180-kD molecule is acidic in nature and highly heterogeneous, whereas the 220-kD protein is neutral and less heterogeneous. Both seem to have 0and N-linked oligosaccharide chains. The 180-kD protein contains 13-16% carbohydrate, whereas the 220-kD molecular contains only 7-8%. Amino acid analysis and peptide mapping also show that each protein represents a unique polypeptide chain. o 1995 Wiley-Liss. Inc.
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