PMID: 2125466Jun 1, 1990Paper

Examination of corneal proteoglycans and glycosaminoglycans by rotary shadowing and electron microscopy

International Journal of Biological Macromolecules
J E ScottS P Damle

Abstract

Proteoglycans (PGs) from cornea and their relevant glycosaminoglycan (GAG) chains, dermatan sulphate (DS) and keratin sulphate (KS), were examined by electron microscopy following rotary shadowing, and compared with hyaluronan (HA), chondroitin sulphate (CS), alginate, heparin, heparan sulphate (HS) and methyl cellulose. Corneal DS PG had the tadpole shape previously seen in scleral DS FG, and the images from corneal KS PG could be interpreted similarly, although the GAG (KS) chains were very much fainter than those of DS PG GAG. Isolated GAG (KS, DS, CS, HA, etc.) examined in the same way showed images that decreased very significantly in clarity and contrast, in the sequence HA greater than DS greater than CS greater than KS. The presence of secondary and tertiary structures in the GAGs may be at least partly responsible for these variations. HA appeared to be double stranded, and DS frequently self-aggregated, KS and HS showed tendencies to coil into globular shapes. It is concluded that it is unsafe to assume the absence of GAGs, based on these techniques, and quantitative measurements of length may be subject to error. The results on corneal DS PG confirm and extend the hypothesis that PGs specifically associated with coll...Continue Reading

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Citations

Apr 27, 1999·The British Journal of Ophthalmology·T KatoA Kanai
Jul 7, 2007·The Clinical Neuropsychologist·Daniel N AllenGerald Goldstein
Feb 26, 2020·PeerJ·Tatyana PonomarevaEvgeny Sogorin
Nov 14, 1997·Journal of Structural Biology·I Pasquali-RonchettiP Ghosh
Dec 1, 1993·The International Journal of Biochemistry·C D Lindsay, J C Anderson
Mar 23, 2005·Carbohydrate Research·Mary K Cowman, Shiro Matsuoka
Feb 19, 2002·Chemical Reviews·Lubomír Lapcík L Jr andPeter Chabrecek
Dec 26, 2001·Biomacromolecules·W E KrauseR H Colby

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