Lysine-specific Porphyromonas gingivalis proteinase
US5707620A · kind A · utility
Assignee
Inventors
Key dates
| Filing date | Oct 10, 1995 |
| Grant date | Jan 13, 1998 |
| Priority date | — |
| Expiry date | Oct 10, 2015 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC12N9/52
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
Provide herein is a substantially pure Lys-gingipain complex preparation, Lys-gingipain being characterized as having an apparent molecular mass of 105 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, where sample is prepared without boiling, said Lys-gingipain having amidolytic and proteolytic activity for cleavage after lysine residues and having no amidolytic and/or proteolytic activity for cleavage after arginine residues, wherein the amidolytic and/or proteolytic activity is inhibited by TLCK, cysteine protease group-specific inhibitors including iodoacetamide and iodoacetic acid, wherein the amidolytic and/or proteolytic activity of said Lys-gingipain is not sensitive to inhibition by leupeptin, antipain, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, serine protease group-specific inhibitors including diisopropylfluorophosphate and phenylmethyl sulfonylfluoride, and antibodies specific for the Lys-gingipain protein complex and its catalytic component, methods for preparation. As specifically exemplified, a Lys-gingipain protein complex is purified from Porphyromonas gingivalis H66, and the 60 kDa catalytic component of the Lys-gingipain …
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