l. Proteoglycans (PGs) in rabbit corneal stroma and mouse sclera have been stained for electron microscopy with Cupromeronic blue in a critical electrolyte concentration (CEC) mode, with and without prior digestion of the tissue by keratanase or chondroitinase ABC to remove the keratan sulphate (KS) or chondroitin-dermatan sulphates (CS or DS) respectively.2. Two classes of PGs, located orthogonally to the corneal collagen fibrils at either the ‘step’ (band ‘a’ or ‘c’) or gap zone (band ‘d’ or ‘e’) are shown to be KS-PGs or DS-PGs respectively. Four separate and specific PG binding sites on Type I collagen fibrils have thus been identified.3. Rabbit corneal KS and DS PGs each contain two kinds of PG (Gregory JD, Coster L & Damle SP (1982) J. Biol. Chem.257, 6965–6970). We propose that each ‘small’ protein-rich PG is associated with a specific binding site on the collagen fibril.
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September 01 1985
‘Small’-proteoglycan: collagen interactions: Keratan sulphate proteoglycan associates with rabbit corneal collagen fibrils at the ‘a’ and ‘c’ bands
J. E. Scott;
J. E. Scott
1Chemical Morphology, University of Manchester, Chemistry Building, Manchesten M13 9PL, UK
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M. Haigh
M. Haigh
1Chemical Morphology, University of Manchester, Chemistry Building, Manchesten M13 9PL, UK
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Publisher: Portland Press Ltd
Received:
September 14 1985
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1985 The Biochemical Society
1985
Biosci Rep (1985) 5 (9): 765–774.
Article history
Received:
September 14 1985
Citation
J. E. Scott, M. Haigh; ‘Small’-proteoglycan: collagen interactions: Keratan sulphate proteoglycan associates with rabbit corneal collagen fibrils at the ‘a’ and ‘c’ bands. Biosci Rep 1 September 1985; 5 (9): 765–774. doi: https://doi.org/10.1007/BF01119875
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