Characterization of heparinase from an oral bacterium Prevotella heparinolytica

Journal of Biochemistry
M WatanabeK Sugahara

Abstract

Heparinase was purified to homogeneity from the cell extract of an oral bacterium, Prevotella heparinolytica, by a combination of anion exchange chromatography, gel filtration chromatography, and hydroxyapatite chromatography. Properties of the purified P. heparinolytica heparinase (P. heparinase) were investigated. The enzyme exhibited a maximum activity in 50 mM Tris-HCl buffer, pH 7.5-8.0, containing 75 mM sodium acetate, 0.1 M NaCl, and 1 mM CaCl2. Optimum conditions for the maximum activity of P. heparinase were similar to those of the heparinase from Flavobacterium heparinum (F. heparinase). The two enzymes also yielded similar digestion profiles of various glycosaminoglycans and heparin tetrasaccharides, suggesting that they have a similar substrate specificity. Kinetic study of the P. heparinase reaction using porcine intestinal heparin as substrate gave a Km value of 3.8 x 10(-5) M and a Vmax value of 11.4 micromol/min x mg protein. The Michaelis constant of P. heparinase was slightly larger than but not significantly different from that of F. heparinase. The amino acid composition of P. heparinase was also similar to that of F. heparinase, but its N-terminal sequence of 20 amino acid residues was different and hithert...Continue Reading

Citations

Dec 1, 1999·Infectious Disease Clinics of North America·G S Schuster
Jul 3, 2002·Bioscience, Biotechnology, and Biochemistry·Eiichi YoshidaYasutaka Tahara
Jul 19, 2003·European Journal of Biochemistry·Sung-Woon HongDong-Hyun Kim
Apr 25, 2015·Chembiochem : a European Journal of Chemical Biology·Lisa BohlmannMark von Itzstein
Jul 1, 2020·Advanced Healthcare Materials·Sufeng ZhangGiovanni Traverso
Mar 10, 2007·Archives of Biochemistry and Biophysics·Yongde LuoWallace L McKeehan

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