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    Examination of the substrate specificity of heparin and heparan sulfate lyases.

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    Authors
    Linhardt, R J
    Turnbull, Jeremy E
    Wang, H M
    Loganathan, D
    Gallagher, John T
    Affiliation
    Division of Medicinal and Natural Products Chemistry, College of Pharmacy, University of Iowa, Iowa City 52242.
    Issue Date
    1990-03-13
    
    Metadata
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    Abstract
    We have examined the activities of different preparations of heparin and heparan sulfate lyases from Flavobacterium heparinum. The enzymes were incubated with oligosaccharides of known size and sequence and with complex polysaccharide substrates, and the resulting degradation products were analyzed by strong-anion-exchange high-performance liquid chromatography and by oligosaccharide mapping using gradient polyacrylamide gel electrophoresis. Heparinase (EC 4.2.2.7) purified in our laboratory and a so-called Heparinase I (Hep I) from a commercial source yielded similar oligosaccharide maps with heparin substrates and displayed specificity for di- or trisulfated disaccharides of the structure----4)-alpha-D-GlcNp2S(6R)(1----4)-alpha-L-IdoAp2S( 1----(where R = O-sulfo or OH). Oligosaccharide mapping with two different commercial preparations of heparan sulfate lyase [heparitinase (EC 4.2.2.8)] indicated close similarities in their depolymerization of heparan sulfate. Furthermore, these enzymes only degraded defined oligosaccharides at hexosaminidic linkages with glucuronic acid:----4)-alpha-D-GlcNpR(1----4)-beta-D-GlcAp(1----(where R = N-acetamido or N-sulfo). The enzymes showed activity against solitary glucuronate-containing disaccharides in otherwise highly sulfated domains including the saccharide sequence that contains the antithrombin binding region in heparin. A different commercial enzyme, Heparinase II (Hep II), displayed a broad spectrum of activity against polysaccharide and oligosaccharide substrates, but mapping data indicated that it was a separate enzyme rather than a mixture of heparinase and heparitinase/Hep III. When used in conjunction with the described separation procedures, these enzymes are powerful reagents for the structural/sequence analysis of heparin and heparan sulfate.
    Citation
    Examination of the substrate specificity of heparin and heparan sulfate lyases. 1990, 29 (10):2611-7 Biochemistry
    Journal
    Biochemistry
    URI
    http://hdl.handle.net/10541/109876
    DOI
    10.1021/bi00462a026
    PubMed ID
    2334685
    Type
    Article
    Language
    en
    ISSN
    0006-2960
    ae974a485f413a2113503eed53cd6c53
    10.1021/bi00462a026
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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