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Vitelline coat of Unio elongatulus: II. Biochemical properties of the 220- and 180-kD components

โœ 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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โœฆ 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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Vitelline coat of Unio elongatulus: III.
โœ R. Focarelli; F. Leotta; R. Lampariello; Dr. Floriana Rosati ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 594 KB

## Abstract Lectins of different binding specificity were used to analyze the oligosaccharide chains of the 220โ€ and 180โ€kD 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