Arginine deiminase from a Mycoplasma arginini strain
AssigneeNippon Mining Co., Ltd.
InventorsKaruo Takaku, Kaoru Miyazaki, Miho Aoshima
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Abstract
A novel arginine deiminase of an approximately 45,000 molecular weight derived from mycoplasma having an ability to decompose arginine, and the method of manufacturing this novel enzyme from mycoplasma. This enzyme is an effective anti-cancer agent, as it shows anti-cancer activities both in vitro and in vivo.
Claims2
A purified arginine deiminase which hydrolyzes the amidino group of L-arginine into L-citrulline and ammonia, and having a molecular weight of approximately 45,000, as determined by SDS-polyacrylamide gel electrophoresis, an iso-electric point of approximately 4.7, and an amino acid sequence as shown in FIGS. 4a, 4b, and 4c.
A purified arginine deiminase obtained from Mycoplasma arginini (IFO catalog No. 14476) and having the following physicochemical properties:
- (a) Function and substrate specificity:
- Hydrolyzes the amidino groups of L-arginine into L-citrulline and ammonia
- (b) Optimum pH:
- 6.0-7.5
- (c) Stable pH:
- 4.5-9.0
- (d) Optimum temperature:
- Approx. 50.degree. C.
- (e) Km value:
- Approx. 0.2 mM
- (f) Isoelectric point (pI):
- Approx. 4.7
- (g) Molecular weight:
- Approx. 45,000
- (by SDS-polyacrylamide gel electrophoresis)
- Approx. 90,000
- (by gel filtration HPLC method)
- (h) Amino acid sequence:
- an amino acid sequence as shown in FIGS. 4a, 4b and 4c.
Dependencies are inferred from the claim text.