Purification of heparinase I, II, and III from Flavobacterium he

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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435183, 435232, 435822, 435850, C12N 900, C12N 952, C12N 120

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053895398

ABSTRACT:
A purified heparinase I, II and III free of lyase activity and each having a molecular weight of 42,800 84,100, 70,800, respectively, are produced by culturing Flavobacterium heparinum. The kinetic properties of the heparinases have been determined as well as the conditions to optimize their activity and stability.

REFERENCES:
patent: 4341869 (1982-07-01), Langer et al.
patent: 4373023 (1983-02-01), Langer et al.
patent: 4396762 (1983-08-01), Langer et al.
patent: 4443545 (1984-04-01), Langer et al.
patent: 5169772 (1992-12-01), Zimmerman et al.
patent: 5198355 (1993-03-01), Kikuchi et al.
Hovingh, P. and Linker, A., "The Enzymatic Degradation of Heparin and Heparitin Sulfate," J. Biol. Chem. 245, 6170-6175 (1970).
Yang, V. C., et al., "Purification and Characterization of Heparinase from Flavobacterium Heparinum," J. Biol. Chem. 260, 1849-1857 (Feb. 1985).
Nakamura, T., et al., "Purification and Properties of Bacteroides Heparinolyticus Heparinase (Heparin Lyase) EC 4.2.2.7)," J. Clin. Microbiol. 26, 1070-1071 (1988).
Ototani, N., et al., "Purification of Heparinase and Heparitinase by Affinity Chromatography on Glycosaminoglycan-Bound AH-Sepharose 4B," Carbohydr. Res. 88, 291-303 (1981).
Galliher, P. M., et al., "Heparinase Production by Flavobacterium Heparinum," Appl. Environ. Microbiol. 41, 360-365 (1981).
Deutscher, M. P. (ed.) "Guide to Protein Purification," Methods in Enzymology 182, 603-613, 738-751.
Berger, S., et al., "Guide to Molecular Cloning Techniques," Methods in Enzymology 152, 393-399, 415-423, 432-447 (1987).
Cerbelaud, E. C., et al., "Sulfur Regulation of Heparinase and Sulfatases in Flavobacterium heparinum," Appl. Environ. Microbiol. 51, 640-646 (Mar. 1986).
Belyavsky, A., et al., "PCR-based cDNA library construction; general cDNA libraries at the level of a few cells," 17, 2919-2932 (Apr. 1989).
Yoshizawa, et al., A 79, 107,584 (Japan) 23 Aug. 1979 CA91:209379d.
Bernstein, H., "A System for Heparin Removal," Ph.D. Dissertation, Massachusetts Institute of Technology (1985).
Charm, S. E., et al., "Scale-Up of Protein Isolation," W. B. Jakobym, ed., Methods in Enzymology 22, 476-490 (Academic Press, New York 1971).
Langer, R., et al., "An Enzymatic System for Removing Heparin in Extracorporeal Therapy," Science 217, 261-263 (Jul. 1982).
Linhardt, R. J., et al., "Immuno-Affinity Purification of Heparinase," Int. J. Biochem. 17(11), 1179-1183 (1985).
Linker, A., et al., "Heparinase and Heparitinase from Flavobacteria," V. Ginsburg, ed., Methods in Enzymology 28, 902-911 (Academic Press, New York 1972).
Silva, M. E., et al., "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 56(4) 965-972 (1974).
Yang, V., et al., "Removal of the Anticoagulant Activities of the Low Molecular Weight Heparin Fractions and Fragments with Flavobacterial heparinase," Thrombosis Research 44(5), 599-610.
Stecher, et al., Ed., The Merck Index, Eighth Ed., 879 (1968).

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