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Literature DB >> 2098717

Purification and characterization of a 43-kDa protease of Bacteroides gingivalis.

Abstract

From the culture supernatant of Bacteroides gingivalis ATCC 33277, a thiol protease was purified to homogeneity by fractional ammonium sulfate precipitation, ion-exchange chromatography, gel filtration, and isoelectric focusing. Its molecular weight was 43 kDa and showed similar enzymatic properties to a 300-kDa protease that was previously characterized.

Entities: Chemical Species

Mesh：

Substances：
Endopeptidases

Year: 1990 PMID： 2098717 DOI： 10.1111/j.1399-302x.1990.tb00441.x

Source DB: PubMed Journal: Oral Microbiol Immunol ISSN： 0902-0055

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Cited

9 in total

1. Binding of hemoglobin to the envelope of Porphyromonas gingivalis and isolation of the hemoglobin-binding protein.

Authors: S Fujimura; Y Shibata; K Hirai; T Nakamura
Journal: Infect Immun Date: 1996-06 Impact factor: 3.441

2. Characterization of Porphyromonas gingivalis-induced degradation of epithelial cell junctional complexes.

Authors: J Katz; V Sambandam; J H Wu; S M Michalek; D F Balkovetz
Journal: Infect Immun Date: 2000-03 Impact factor: 3.441

3. Isolation and characterization of the Porphyromonas gingivalis prtT gene, coding for protease activity.

Authors: J Otogoto; H K Kuramitsu
Journal: Infect Immun Date: 1993-01 Impact factor: 3.441

4. The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain.

Authors: J Potempa; R Pike; J Travis
Journal: Infect Immun Date: 1995-04 Impact factor: 3.441

5. Purification and characterization of a protease from Porphyromonas gingivalis capable of degrading salt-solubilized collagen.

Authors: H T Sojar; J Y Lee; G S Bedi; R J Genco
Journal: Infect Immun Date: 1993-06 Impact factor: 3.441

Purification and characterization of a 43-kDa protease of Bacteroides gingivalis.

1. Binding of hemoglobin to the envelope of Porphyromonas gingivalis and isolation of the hemoglobin-binding protein.

2. Characterization of Porphyromonas gingivalis-induced degradation of epithelial cell junctional complexes.

3. Isolation and characterization of the Porphyromonas gingivalis prtT gene, coding for protease activity.

4. The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain.

5. Purification and characterization of a protease from Porphyromonas gingivalis capable of degrading salt-solubilized collagen.

6. Purification and characterization of three types of proteases from culture supernatants of Porphyromonas gingivalis.

7. Involvement of arginine-specific cysteine proteinase (Arg-gingipain) in fimbriation of Porphyromonas gingivalis.

8. Analysis of the prtP gene encoding porphypain, a cysteine proteinase of Porphyromonas gingivalis.

9. Cellular locations of proteinases and association with vesicles in Porphyromonas gingivalis.