The sulphation pattern in chondroitin sulphate chains investigated by chondroitinase ABC and ACII digestion and reactivity with monoclonal antibodies

التفاصيل البيبلوغرافية
العنوان: The sulphation pattern in chondroitin sulphate chains investigated by chondroitinase ABC and ACII digestion and reactivity with monoclonal antibodies
المؤلفون: Paula K. Hazell, Timothy E. Hardingham, Roger J.F. Ewins, Amanda J. Fosang, Nina J. Hey, Wai Jing Kee
المصدر: Carbohydrate Research. 255:241-254
بيانات النشر: Elsevier BV, 1994.
سنة النشر: 1994
مصطلحات موضوعية: Swine, Molecular Sequence Data, Disaccharide, Chondroitin ABC lyase, Biochemistry, Analytical Chemistry, Epitopes, chemistry.chemical_compound, Sulfation, Antibody Specificity, Animals, Lectins, C-Type, Aggrecans, Chondroitin sulfate, Aggrecan, chemistry.chemical_classification, Extracellular Matrix Proteins, Chromatography, Chondroitin Lyases, Chondroitin Sulfates, Organic Chemistry, Antibodies, Monoclonal, General Medicine, Enzyme, Carbohydrate Sequence, Chondroitin Sulfate Proteoglycans, chemistry, Proteoglycans, Digestion, Chondroitin AC lyase
الوصف: We have used progressive chondroitinase digestion of pig aggrecan in conjunction with ELISA assays and disaccharide analysis to derive information about the pattern of 4- and 6-sulphation in chondroitin sulphate chains. Digestion with chondroitinase ABC resulted in the release of mainly disaccharides from the nonreducing terminal of chondroitin sulphate chains but there was also the release of some tetra- and hexa-saccharides which were degraded to disaccharides with more extensive digestion. Chondroitinase ACII, in contrast, released only disaccharides. Analysis of the disaccharide composition of the intact and digested products at different stages of digestion showed that there was a slight increase in 6-sulphate content of the chains as they were shortened. Reaction of the partially digested proteoglycans with monoclonal antibodies 3-B-3 and 3-D-5 which recognise chains terminating in 6- or 4-sulphated disaccharides, respectively, showed major differences between chondroitinase ABC and ACII products. The results suggested that chondroitinase ABC preferentially cleaved next to 4-sulphated, rather than 6-sulphated disaccharides and this resulted in some oligosaccharides as well as disaccharide being released. Chondroitinase ACII also cleaved an additional disaccharide next to the linkage to protein of chondroitin sulphate, which was not removed by chondroitinase ABC and this disaccharide was mainly nonsulphated.
تدمد: 0008-6215
DOI: 10.1016/s0008-6215(00)90982-0
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15150b8707861f257fc891c280c432f7
https://doi.org/10.1016/s0008-6215(00)90982-0
Rights: CLOSED
رقم الانضمام: edsair.doi.dedup.....15150b8707861f257fc891c280c432f7
قاعدة البيانات: OpenAIRE
الوصف
تدمد:00086215
DOI:10.1016/s0008-6215(00)90982-0