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The Adhesive Glycoprotein of the Orb Web of Argiope Aurantia (Araneae, Araneidae)

Published online by Cambridge University Press:  15 February 2011

Edward K. Tillinghast ,
Mark A. Townley ,
Thomas N. Wight ,
Gerhard Uhlenbruck  and
Eveline Janssen
Edward K. Tillinghast
Affiliation:
University of New Hampshire, Department of Zoology, Durham, NH 03824USA
Mark A. Townley
Affiliation:
University of New Hampshire, Department of Zoology, Durham, NH 03824USA
Thomas N. Wight
Affiliation:
University of Washington, Department of Pathology, Seattle, WA 98195USA
Gerhard Uhlenbruck
Affiliation:
Universitäat zu Köln, Institut für Immunbiologie, Kerpener Straβe 15, D- 5000 Köln 41, Germany.
Eveline Janssen
Affiliation:
Universitäat zu Köln, Institut für Immunbiologie, Kerpener Straβe 15, D- 5000 Köln 41, Germany.
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Abstract

A phosphorylated, glycoprotein preparation has been obtained from orb webs of the araneid spider Argiope aurantia. This preparation probably contains proteins from more than one gland type, but resolution of these proteins has not yet been achieved. Nevertheless, a major component appears to be the adhesive glycoprotein(s) from the adhesive spiral. A product of the aggregate glands, this glycoprotein(s) occurs as discrete nodules along the core fibers of the adhesive spiral, within the viscid, aqueous droplets.

The glycoprotein preparation has a high apparent molecular weight (> 200 kDa) and is polydisperse. The only monosaccharide constituent identified by gas-liquid chromatography or in lectin studies is N-acetylgalactosamine and this is at least primarily O-linked to threonine. By electron microscopy, linear, unbranched and apparently flexible filaments are observed. Phosphorylated serine and threonine residues are present in the preparation and glycine, proline and threonine together account for about 57 mole % of the preparation's amino acid content. Thus, in some, but not all, respects, this glycoprotein preparation is reminiscent of a secretory mucin.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 292: Symposium S – Biomolecular Materials , 1992 , 9
Copyright
Copyright © Materials Research Society 1993

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