Acidic glycosaminoglycans, isolation and structural analysis of a proteodermatan sulfate from dermatosparactic calf skin
- PMID: 3581752
- DOI: 10.1016/s0174-173x(87)80046-8
Acidic glycosaminoglycans, isolation and structural analysis of a proteodermatan sulfate from dermatosparactic calf skin
Abstract
Dermatan sulfate and hyaluronic acid are the major glycosaminoglycan components of dermatosparactic and normal calf skin but the ratio of hyaluronic acid to dermatan sulfate is 50-70% higher in dermatosparactic calf skin than that in normal calf skin. Hyaluronic acid in normal calf skin could be extracted to 93% of the total by NaCl and guanidine hydrochloride, while in dermatosparactic calf skin 57% of hyaluronic acid remained in the insoluble material after NaCl and guanidine hydrochloride extraction. The recovery of proteodermatan sulfate in NaCl extracts was similar in normal and dermatosparactic skin. The amount of proteodermatan sulfate extracted in guanidine hydrochloride form normal calf skin was 2-4 fold higher than that from dermatosparactic calf skin. No significant difference between dermatosparactic and normal calf skin proteodermatan sulfate could be detected in terms of size of the core protein (Mr = 55,000) by sodium dodecyl sulfate polyacrylamide gel electrophoresis, amino acid analysis, immunological cross-reactivity using polyclonal antibodies against either dermatosparactic or normal calf skin core protein, tryptic peptides or size of dermatan sulfate chains (Mr = 17,000-18,000) on gel chromatography.
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