New insights on the specificity of heparin and heparan sulfate lyases from Flavobacterium heparinum revealed by the use of synthetic derivatives of K5 polysaccharide from E. coli and 2-O-desulfated heparin.

This publication has 23 references indexed in Scilit:

• Domain Structure of Heparan Sulfates from Bovine Organs
  Journal of Biological Chemistry, 1996
• Specificity studies on the heparin lyases from Flavobacterium heparinum
  Biochemistry, 1993
• Effect of monensin on the sulfation of heparan sulfate proteoglycan from endothelial cells
  Journal of Cellular Biochemistry, 1992
• Heparin in molluscs: chemical, enzymatic degradation and 13C and 1H n.m.r. spectroscopical evidence for the maintenance of the structure through evolution
  International Journal of Biological Macromolecules, 1989
• Structural studies and “in vivo” and “in vitro” pharmacological activities of heparin fractions and fragments prepared by chemical and enzymic depolimerization
  Thrombosis Research, 1985
• Structural studies on heparin. Tetrasaccharides obtained by heparinase degradation
  Carbohydrate Research, 1984
• Structural differences of heparan sulfates according to the tissue and species of origin
  Biochemical and Biophysical Research Communications, 1983
• The Structure of the Capsular Polysaccharide (K5 Antigenn) of Urinary-Tract-Infective Escherichia coli 010:K5:H4. A Polymer Similar to Desulfo-Heparin
  European Journal of Biochemistry, 1981
• Fractionation and properties of four heparitin sulfates from beef lung tissueIsolation and partial characterization of a homogeneous species of heparitin sulfate
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1974
• Isolation and partial characterization of three induced enzymes from flavobacterium heparinum involved in the degradation of heparin and heparitin sulfates
  Biochemical and Biophysical Research Communications, 1974