A comparative analysis of the primary sequences and characteristics of heparinases I, II, and III from Flavobacterium heparinum.

@article{Godavarti1996ACA,
  title={A comparative analysis of the primary sequences and characteristics of heparinases I, II, and III from Flavobacterium heparinum.},
  author={R Godavarti and Ram Sasisekharan},
  journal={Biochemical and biophysical research communications},
  year={1996},
  volume={229 3},
  pages={770-7}
}
Heparinases I, II and III from F. heparinum cleave heparin-like molecules, with a high degree of substrate specificity, at the glucosamine-uronate linkage by elimination, leaving an unsaturated C4-C5 bond in the uronic acid. The primary sequences of these enzymes have been reported earlier. In this study we perform a comparative analysis of the properties and primary sequences of heparinase I, II and III. Alignment of the primary sequences revealed little sequence homology (15% residue identity… CONTINUE READING

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