Chemistry: molecular biology and microbiology – Process of utilizing an enzyme or micro-organism to destroy... – Treating animal or plant material or micro-organism
Patent
1991-04-04
1993-11-16
Naff, David M.
Chemistry: molecular biology and microbiology
Process of utilizing an enzyme or micro-organism to destroy...
Treating animal or plant material or micro-organism
435200, 435 13, C07K 300, C12N 924, C12Q 156
Patent
active
052623254
ABSTRACT:
A heparinase formulation derived from Flavobacterium heparinum which meets all requirements for a clinical reagent that can eliminate heparin interference of normal blood function has been developed. The heparinase, derived from Flavobacterium heparinum, is free of a component that inhibits coagulation. It is stable under normal manufacturing, shipping and clinical storage conditions for at least one year. The heparinase in useful in vitro to eliminate the interference in hematological assays due to the presence of heparin. The heparinase is also useful for the in vivo neutralization of heparin during surgical procedures. Advantages of this preparation are that it achieves neutralization faster and more completely than previously available compositions and is stable for long periods of time.
REFERENCES:
patent: 3950133 (1976-04-01), Monte et al.
patent: 4795703 (1989-01-01), Folkman et al.
Lindahl, et al., "Biosynthesis of Heparin" TIBS 11(5):221-225, (1986).
Sakamoto, et al., "Heparin and bone Metabolism: Effects of heparin on bone collagenase release and activity and an application of heparin-sepharose affiity chromatography for in vitro study of bone resorption" Chemistry and Biology of Heparin; (Elsevier/North Holland Press, Amsterdam 1981).
Rosenberg, et al., "The purification and mechanism of action of the human antithrombin-heparin cofactor"; J. Biol. Chem., 248:6490-6505.
Cumming, A. M., et al., "In vitro neutralization of heparin in plasma prior to the activated partial thromboplastin time test; an assessment of four heparin antagonists and two anion exchange resins" Thrombosis Res., 41:43-56.
Funk, C., et al., "Reptilase-R--a new reagent in blood coagulation" Brit. J. Haematol., 21:43-52.
Hutt, Ed, et al., "Use of Heparinase to eliminate heparin inhibition in routine coagulation assays" J. Lab. Clin. Med. 79:1027, 1972.
Akoum, A., et al., "Anticoagulant activity of a bacterial glycopeptide" Thrombosis Res., 60: 9-18.
Galliher, P. C., et al. "Heparinase production by Flavobacterium herpainum" Appl. Envir. Microbiol., 41(2):360-365.
Bohmer, L. H., et al., "Heparin degradation by a novel heparinase" Thrombosis Res. 60:331-335.
Klein, et al., "Heparinase. Invivo activity and immunogenecity in rabbits" J. Lab. Clin. Med., 102:8280837.
Langer, et al., "In vivo activity of microbial heparinase" Trans Am Soc Artific Intern Organs, 28:387-390.
Fabian, et al. "Polycations as Possible Substitutes for Protamine in Heparin Neutralization", Thrombosis Research, 17:239-247, (Pergamon Press Ltd. 1980).
Langer, et al., "An Enzymatic System for Removing Heparin in Extra-Corporeal Therapy", Science, vol. 271, 261-263, (Jul. 16, 1982).
Dixon et al., Enzymes, Fractionation Methods, p. 39, 1964.
Heft Robert A.
Lewis N. Tracey
Zimmermann Joseph J.
Ibex Technologies, Inc.
Meller Michael
Naff David M.
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