Heparinase I from Flavobacterium heparinum. Mapping and characterization of the heparin binding domain

In this study we have identified the primary heparin binding site of heparinase I (EC 4.2.2.7). Chemical and proteolytic digests of heparinase I were used in direct binding and competition assays, to map the regions of heparinase I that interact specifically with heparin. We find the heparin binding...

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Veröffentlicht in:	The Journal of biological chemistry 1996-02, Vol.271 (6), p.3124-3131
Hauptverfasser:	Sasisekharan, R, Venkataraman, G, Godavarti, R, Ernst, S, Cooney, C L, Langer, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Base Sequence Binding Sites Carbohydrate Conformation Carbohydrate Sequence Chromatography, Affinity Chromatography, High Pressure Liquid Cloning, Molecular Consensus Sequence Cyanogen Bromide DNA Primers Flavobacterium - enzymology Flavobacterium heparinum Heparin - metabolism Heparin Lyase Molecular Sequence Data Mutagenesis, Site-Directed Peptide Fragments - chemistry Point Mutation Polymerase Chain Reaction Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - isolation & purification Polysaccharide-Lyases - metabolism Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Trypsin
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