Abstract
Human corneas from normal (healthy) donors and patients with keratoconus were either metabolically labelled under organ culture conditions or investigated without preincubation. The sulfated proteoglycans were isolated from a 4 M guanidinium chloride/2% Triton X 100 extract. Two predominant proteoglycans were obtained from normal cornea after digestion of total sulfated proteoglycans with chondroitin ABC-lyase or endo-beta-galactosidase. One had an overall mass of 150 kDa, two dermatan sulfate chains (Mr approximately 50 kDa) with an iduronic acid content of 24%-28% and, after chondroitin ABC-lyase digestion, a core protein of 48 kDa. The other proteoglycan had an overall mass of 110 kDa, one keratan sulfate chain of approximately 60 kDa and, following endo-beta-galactosidase (keratanase) digestion, a core protein of 46 kDa. Each proteoglycan population was further fractionated into two subpopulations by chromatography on concanavalin A-Sepharose. The dermatan sulfate- and keratan sulfate-containing proteoglycans isolated from keratan and healthy cornea had comparable Mr values and core proteins with identical molecular weights, but the ratio of dermatan sulfate/keratan sulfate proteoglycan was increased in keratoconic cornea a...Continue Reading
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