Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Hydrolases
Reexamination Certificate
2011-05-24
2011-05-24
Peng, Bo (Department: 1648)
Drug, bio-affecting and body treating compositions
Enzyme or coenzyme containing
Hydrolases
C435S183000
Reexamination Certificate
active
07947270
ABSTRACT:
The invention relates to a multifunctional enzyme that can be derived from crustaceans or fish. The enzyme has at least one of a chymotrypsin, trypsin, elastase, collagenase and exo peptidase activity, and a molecular weight between about 20 kd and about 40 kd as determined by SDS PAGE. Preferably, the multifunctional enzyme has substantial anti cell-cell adhesion activity. Preferably, the multifunctional enzyme has substantial homology with the krill multifunctional enzyme. These enzymes are useful for treating viral infections such as herpes outbreaks, fungal, bacterial or parasitic infections, including the primary and secondary infections of leprosy, colitis, ulcers, hemorrhoids, corneal scarring, dental plaque, acne, cystic fibrosis, blood clots, wounds, immune disorders including autoimmune disease and cancer. Additionally, the invention relates to a method of purifying the multifunctional enzyme, and to a preparation of essentially purified multifunctional enzyme.
REFERENCES:
patent: 4677069 (1987-06-01), Chen et al.
patent: 4801451 (1989-01-01), Hellgren et al.
patent: 4837009 (1989-06-01), Ractliff
patent: 4963491 (1990-10-01), Hellgren et al.
patent: 5134119 (1992-07-01), Lezdey John et al.
patent: 5439935 (1995-08-01), Rawlings et al.
patent: 5945102 (1999-08-01), de Faire et al.
patent: 5958406 (1999-09-01), de Faire et al.
patent: 6030612 (2000-02-01), de Faire et al.
patent: 2006/0134641 (2006-06-01), Franklin
patent: 0170115 (1985-07-01), None
patent: 0 257 003 (1988-02-01), None
patent: 9319732 (1993-10-01), None
patent: 9324142 (1993-12-01), None
patent: 9419005 (1994-09-01), None
patent: 9507686 (1995-03-01), None
patent: 9507688 (1995-03-01), None
Definitions for Glycosaminoglycan and Glucosaminoglycan, On-Line Medical Dictionary, CancerWEB 1997-2002.
Rathgeber WF, S. Afr. Med. J., (45(7):181-183 (1971) [English].
Coblentz, J. Am. Geriatr Soc., 16(9):1039-1046 (1968) [English].
Grant and Eisen, Substrate Specificity of the Collagenolytic Serine Protease from Uca Pugilator: Studies with Noncollagegenous Substrates, Biochemistry, 19:6089-6095 (1980).
Grant et al., Collagenolytic Protease from Fiddler Crab (Uca Pugilator), Methods in Enzymology, 80:722-734 (1980).
Grant et al., A Collagenolytic Serine Protease with Trypsin-Like Specificity from the Fiddler Crab Uca Pugilator, Biochemistry, 22:354-358 (1983).
Welgus and Grant, Degradation of Collagen Substrates by a Trypsin-Like Serine Protease from the Fiddler Crab Uca Pugilator, Biochemistry, 22:2228-2233 (1983).
Al-Mohanna et al., Mitotic E- and Secretory F-Cells in the Hepatopancreas of the Shrimp Penaeus Semisulcatus (Crustacea: Decapoda), J. Mar. Biol. Ass. U.K., 65:901-910 (1985).
Lipman and Pearson, Rapid and Sensitive Protein Similarity Searches, Science, 227:1435-1441 (Mar. 22, 1985).
Gudmundsodottir et al., Isolation and Characterization of cDNAS from Atlantic Cod Encoding Two Different Forms of Trypsinogen, Eur. J. Biochem., 217, 1091-1097 (1993).
Lu et al., The Midgut Trypsins of Shrimp (Penaeus Monodon), Biol. Chem. Hoppe-Seyler, 371:851-859 (Sep. 1990).
Turkiewicz et al., Collagenolytic Serine Proteinase from Euphausia Superba Dana (Antarctic Krill), Comp. Biochem. Physiol., 99B:359-371 (1991).
Tsai et al., The Midgut Chymotrypsins of Shrimps (Penaeus Monodon, Penaeus Japonicus and Penaeus Penicillatus) Biochimica et Biophysica Acta, 1080:59-67 (1991).
Wormhoudt et al., Purification, Biochemical Characterization and N-Terminal Sequence of a Serine-Protease with Chymotrypsic and Collagenolytic Activities in a Tropical Shrimp, Penaeus Vannamei (Crustacea, Decapoda), Comp. Biochem. Physiol., 103B(3):675-680 (1992).
Sellos and Wormhoudt, Molecular Cloning of a cDNA that Encodes a Serine Protease with Chymotryptic and Collagenolytic Activities in the Hepatopancreas of the Shrimp Penaeus Vanameii (Crustacea, Decapoda), FEBS, 309 (3):219-224 (Sep. 1992).
Klimova et al., The Isolation and Properties of Collagenolytic Proteases from Crab Hepatopancreas, Biochemical and Biophysical Research Communications, 166(3):1411-1420 (Feb. 1990).
Tsu et al., The Substrate Specificity of Uca Pugilator Collagenolytic Serine Protease 1 Correlates with the Bovine Type I Collagen Cleavage Sites, The Journal of Biochemical Chemistry, 269(30)19565-19572 (1994).
A. Bucht et al., Immunological Characterization of Three Highly Purified Trypsin-Like Enzymes from Antarctic Krill (Euphausia Superba), Biol. Chem. Hoppe Sryler, 367:366, Abstract 06.03.55 (1986).
Turkiewicz et al., Purification and Characterization of a Proteinase from Euphausia Superba Dana (Antarctic Krill), Acta Biochimica Polonica, 33(2):87-89 (1986).
Chen et al., Purification and Properties of Trypsin-Like Enzymes and a Carboxypeptidase A From Euphausia Superba, Journal of Food Biochemistry, 2:349-366 (1978).
Kimoto et al., Purification and Characterization of Serine Proteinases from Euphasia Superba, Agric. Biol. Chem., 47 (3):529-534 (1983).
Knut Kr. Osnes et al., On the Purification and Characterization of Three Anoinic, Serine-Type Peptide Hydrolases from Antarctic Krill, Euphausia Superba, Comp. Biochem. Physiol., 82B(4):607-619 (1995).
Knut Kr. Osnes et al., On the Purification and Characterization of Exopeptidases from Antarctic Krill, Euphausia Superba, Comp. Biochem. Physiol., 83B(2):445-458 (1986).
Knut Kr. Osnes et al., Hydrolysis of Proteins by Peptide Hydrolases of Antarctic Krill, Euphausia Superba, Comp. Biochem. Physiol., 83B(4):801-805, (1986).
Knut Kr. Osnes et al., Peptide Hydrolases of Antarctic Krill, Euphausia Superba, Comp. Biochem. Physiol, 82B (4):599-606, (1985).
Olav Seather et al., Proteolysis Post Mortem in North Atlantic Krill, Comp. Biochem. Physical, 88B(1):165-176 (1987).
J. Melrose et al., Evauation of Digestive Proteinases from the Antarctic Krill Euphausia Superba, as Potential Chemonucleolytic Agents, Arch Orthop Trauma Surg., 114:145-152 (1995).
Y. Sakharov, Potent Debriding Ability of Collagenolytic Protease Isolated from the Hepatopancreas of the King Crab Paralithodes Camtschatica, Arch Dermatol Res., 285:32-35 (1993).
Arthur Z. Eisen, A Collagenolytic Protease from the Hepatopancreas of the Fiddler Crab, UCA Pugilator, Purification and Properties, Biochemistry, 12(9):1814-1822 (1973).
Asuncion Olalla et la:, Purification and Properties of Three Proteases from the Larvae of the Brine Shrimp Artemia Salina, Biochimica et Biophysica Acta, 523:181-190 (1978).
Spindler et al., Partial Characterization of Chitin Degrading Enzymes from Two Euphausiids, Euphausia Superba, and Meganyctiphanes Norvegica, Polar Biology, 9:115-122 (1988).
Karlstam and Ljunglof, Detection and Partial Purification of a Hyaluronic Acid-Degrading Enzyme from Antarctic Krill (Euphausia Superba, ), Biol. Chem. Hoppe Seyler, 367:339 (1986).
Kimoto et al., Acid Proteinases from Antarctic Krill, Euphausia Superba: Partial Purification and Some Properties, Journal of Food Science, 46:1881-1884 (1981).
Kraft and Falkenberg, Biol. Chem. Hoppe Seyler, 353:1540-1541 (1972).
Sakharov et al., Purification and Characterization of Two Serine Collagenolytic Proteases from Crab Paralithodes Camtschatica, Comp. Biochem. Physiol., 108B:561-568 (1994).
Gates et al., Isolation of Comparative Properties of Shrimp Trypsin, Shrimp Trypsin, 8(11):4483-4489 (1969).
Jacobs, J Am Podiatry Assoc., 55(11):743-746 (1965) [English].
Goodfriend, J Am Podiatry Assoc., 55(9):667-669 (1965) [English].
Arcimboldo AB
Knoble & Yoshida & Dunleavy LLC
Peng Bo
LandOfFree
Removing dental plaque with krill enzymes does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Removing dental plaque with krill enzymes, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Removing dental plaque with krill enzymes will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2654397