The alkali-labile linkage between keratan sulphate and protein

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Chondroitin sulphate and keratan sulphate are almost isosteric.

Keratan sulphate and chondroitin sulphate (KS and CS) in the 2-fold helical configurations that are prevalent in solution are of very similar tacticity. The chiral centres, anionic sites and hydrophobic patches are in identical conformations. Only the position of the acetamido group varies from CS to KS, but part of its intramolecular H-bonding potential in CS is retained in KS. The formation o...

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The linkage region of cartilage keratan sulfate to protein.

Glycopeptides derived from bovine nasal septum keratan sulfate by acid hydrolysis and gel chromatography are shown to be enriched in the carbohydrate-protein linkage region. The effects of alkali on these glycopeptides are compared to the effects on the starting material. It is shown that the 0 elimination caused by alkali is consistent with an O-glycosidic linkage between threonine or serine i...

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Two linkage-region fragments isolated from skeletal keratan sulphate contain a sulphated N-acetylglucosamine residue.

Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (6-year-old animals) after chondroitin ABC lyase digestion followed by digestion of A1D1 proteoglycans by diphenylcarbamoyl chloride-treated trypsin and gel-permeation chromatography on Sepharose CL-6B. Treatment of these peptido-keratan sulphate fragments with alkaline NaB3H4 yielded kerat...

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The effect of mucopolysaccharide linkage region and intrachain alkali labilities on chain weight determination.

The validity of the reducing end group (copper reduction) method for determination of chain weight of chondroitin sulfate is shown by comparison with chain weight determination from linkage region components, xylose and galactose. It is established that chains of both chondroitin sulfate and keratan sulfate are stable to alkali as strong as 2.0 N NaOH at room temperature for at least 120 hours....

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Structure of oligosaccharides and the linkage region between keratan sulfate and the core protein on proteoglycans from monkey cornea.

Structural analyses were performed on the intact glycopeptides and on the linkage region oligosaccharide-peptides derived from the keratan sulfate proteoglycan from monkey cornea (Nakazawa, K., Newsome, D.A., Nilsson, B., Hascall, V.C., and Hassell, J.R. (1983) J. Biol. Chem. 258, 6051-6055) using trifluoroacetolysis, Smith degradation, chromium trioxide oxidation, and gas-liquid chromatography...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1974

ISSN: 0264-6021

DOI: 10.1042/bj1410057