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pubmed-article:3363539pubmed:abstractTextPolysulphated chromatographic media, particularly Heparin Sepharose, are generally used to purify a variety of different plasma proteins. Heparin Sepharose, dextran sulphate Sepharose and sulphated dextran are compared with two recently available sulphated cellulose chromatographic media. The potential influence of structural features of different polysaccharides on the interaction with selected plasma proteins has been evaluated with the particular objective of developing an alternative medium for the preparation of specific therapeutic factor concentrates. The studies indicate that the degree of sulphation of the matrix is an important but not a critical determinant for resolution of factors IX and X. Despite large differences in the carbohydrate structure of the matrices, the new sulphated cellulose gel 5.2 had a total protein capacity and specific binding profile comparable to Heparin Sepharose. The sulphated cellulose which is competitively priced, and has excellent stability, is a potential alternative to Heparin Sepharose especially for larger scale industrial processing of factor IX concentrate.lld:pubmed
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pubmed-article:3363539pubmed:authorpubmed-author:BennyA GAGlld:pubmed
pubmed-article:3363539pubmed:authorpubmed-author:PrestonJJlld:pubmed
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pubmed-article:3363539pubmed:pagination277-86lld:pubmed
pubmed-article:3363539pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:3363539pubmed:year1988lld:pubmed
pubmed-article:3363539pubmed:articleTitleComparative separation of human plasma proteins on polysulphated chromatographic media.lld:pubmed
pubmed-article:3363539pubmed:affiliationRegional Blood Transfusion Centre, Auckland, N.Z.lld:pubmed
pubmed-article:3363539pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3363539pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed