Two dermatan sulphate-containing proteoglycans from bovine sclera were examined by rotary shadowing and electron microscopy, and the results were compared with previous biochemical findings. Both the large iduronate-poor proteoglycan (PGI) and the small iduronate-rich proteoglycan (PGII) possessed a globular proteinaceous region. Whereas PGI had a branched extension from the globular region, with five to eight side chains attached to it, PGII had only a single tail, which was of glycosaminoglycuronan. PGII aggregated via globular-region interactions, which were much diminished by reduction and alkylation. PGI aggregated via side chains and globular-region interactions. Although a few PGI aggregates were large, and similar to the hyaluronan-cartilage proteoglycan aggregates [Weidemann, Paulsson, Timpl, Engel & Heinegård (1984) Biochem. J. 224, 331-333], hyaluronan did not cause enhanced aggregation. PGII is very similar in shape to the small cartilage chondroitin sulphate proteoglycan, whereas PGI somewhat resembles the large cartilage chondroitin sulphate proteoglycan, although with many fewer glycosaminoglycan side chains, and probably only one globular region as opposed to two in the cartilage proteoglycan.
Skip Nav Destination
Close
Article navigation
March 1987
- Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkAdvertising
Research Article|
March 15 1987
Dermatan sulphate proteoglycans from sclera examined by rotary shadowing and electron microscopy
Biochem J (1987) 242 (3): 761–766.
Citation
N P Ward, J E Scott, L Cöster; Dermatan sulphate proteoglycans from sclera examined by rotary shadowing and electron microscopy. Biochem J 15 March 1987; 242 (3): 761–766. doi: https://doi.org/10.1042/bj2420761
Download citation file:
Close
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Cited By
Related Articles
Cartilage proteoglycans. Assembly with hyaluronate and link protein as studied by electron microscopy
Biochem J (July,1988)
Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates
Biochem J (April,1995)
Isolation and characterization of two sialoproteins present only in bone calcified matrix
Biochem J (December,1985)