𝔖 Bobbio Scriptorium
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Vitelline coat of Unio elongatulus egg: I. Isolation and biochemical characterization

✍ Scribed by Riccardo Focarelli; Floriana Rosati

Book ID
111662464
Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
985 KB
Volume
35
Category
Article
ISSN
1040-452X

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πŸ“œ SIMILAR VOLUMES

Vitelline coat of Unio elongatulus: II.
Vitelline coat of Unio elongatulus: II. Biochemical properties of the 220- and 180-kD components
✍ R. Focarelli; A. Santucci; R. Lampariello; Dr. Floriana Rosati πŸ“‚ Article πŸ“… 1995 πŸ› John Wiley and Sons 🌐 English βš– 570 KB

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 iso

Vitelline coat of Unio elongatulus: III.
Vitelline coat of Unio elongatulus: III. Glycan chain analysis of the 220- and 180-kD components by means of lectins
✍ R. Focarelli; F. Leotta; R. Lampariello; Dr. Floriana Rosati πŸ“‚ Article πŸ“… 1995 πŸ› John Wiley and Sons 🌐 English βš– 594 KB

## Abstract Lectins of different binding specificity were used to analyze the oligosaccharide chains of the 220‐ and 180‐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