Isolation and characterization of proteases from Bacteroides melaninogenicus

Fujimura, Setsuo; Nakamura, Takeshi

doi:10.1128/iai.33.3.738-742.1981

Cited by 25 publications

(8 citation statements)

References 29 publications

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“…The result shown maximum activity of enzyme at 45 and these is a sharp decrease in the enzyme activity at 65 °C. these result were in agreement with the other results (Fujimura and Nakamura, 1987;Jram et al, 2007) . Fig.…”

Section: Effect Of Temperature On Protenase Activity: 4-supporting

confidence: 94%

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Partial Separation and some Kinetic Studies of Protenase Enzyme from Human Plasma

Jarah¹,

Israa²

2012

RJS

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This study includes an isolation and partial purification the protenases from human plasma in city center of Mosul. Three proteinous components had been isolated by gel filtration technique from the precipitate produced by saturation ammonium sulfate. It was found that the peak (A) had a high activity of protenases using sephadex G-75. The apparent molecular weight of the isolated protenases the peak (A) using gel filtration was (75000± 1000 Da). Maximum activity for protenases was obtained using (0.32) mM of casein as substrates, phosphate buffer (50 mmol) at PH (7.5) for (10) minutes in incubation at (45) °C. Using Line Weaver-burk plot were the maximum velocity (0.796) U/ml and Michaelis constant (0.035) mmol. EDTA and thiourea inhibition on the protenase activity, while magnesium sulfate and calcium chloride shown increase activity.

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Section: Effect Of Temperature On Protenase Activity: 4-supporting

confidence: 94%

“…4). These results were similar to those how found by other investigators (Fujimura and Nakamura, 1987;Jram et al, 2007).…”

Section: -Effect Of Ph On the Protenase Activitysupporting

confidence: 93%

Partial Separation and some Kinetic Studies of Protenase Enzyme from Human Plasma

Jarah¹,

Israa²

2012

RJS

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“…Before electrophoresis the bacterial cells were separated from the sera by centrifugation and appropriately diluted. Samples (5 pul) of the sera were applied into 2.5-mm wells in a 1% agarose gel (HSA; Litex, Glostrup, Denmark) in Tris-barbital buffer (pH 8.6). The electrophoresis was carried out at 10 V cm-' for 4 h with the same buffer.…”

Section: Methodsmentioning

confidence: 99%

Degradation of the human proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin by Bacteroides gingivalis

Carlsson¹,

Herrmann²,

Höfling³

et al. 1984

Infect Immun

142

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Various strains of black-pigmented Bacteroides species were grown on horse blood agar and suspended in human serum. After various times of incubation the effect of the bacteria on the serum was evaluated by polyacrylamide gel electrophoresis and "rocket" immunoelectrophoresis. The formation of trichloroacetic acid-soluble material in the suspensions and the capacity of the treated sera to inhibit the activity of trypsin were also determined. The two tested strains of Bacteroides gingivalis (W83, H185) degraded most serum proteins, including the plasma proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin. They did not, however, degrade alpha-1-antichymotrypsin. Bacteroides intermedius NCTC 9336, Bacteroides asaccharolyticus NCTC 9337, and an asaccharolytic oral strain different from B. gingivalis (BN11a-f) did not degrade the plasma proteinase inhibitors. These strains were, however, able to inactivate the capacity of serum to inhibit the activity of trypsin.

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“…Such enzymes produced by Bacteroides gingivalis as (ttypsin-like) protease and collagenase are thought to be potent pathogenic factors in periodontal disease (7). We demonstrated earlier the presetice of 2 kinds of caseinolytic enzymes of a strain of Bacteroides melaninogenieus, isolated from the gitigival crevice (3). Recently, many reports on purification and properties of protease, collagenase, and collagenase-related enzymes have appeared in rapid succession (1,4,5,6,(8)(9)(10)(11)(12)(13)(14)(15).…”

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confidence: 76%

Multiple forms of proteases of Bacteroides gingivalis and their cellular location

Fujimura

Nakamura

1989

Oral Microbiology and Immunology

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Protease of Bacteroides gingivalis ATCC 33277 was found in intracellular membrane‐free, intracellular membrane‐bound and extracellular fractions. The insoluble form of proteases was solubilized with a detergent. The elution patterns of proteases on gel filtration in each fraction were rather different. However, enzymatic properties of the proteases separated by gel filtration were very similar.

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Isolation and characterization of proteases from Bacteroides melaninogenicus

Cited by 25 publications

References 29 publications

Partial Separation and some Kinetic Studies of Protenase Enzyme from Human Plasma

Partial Separation and some Kinetic Studies of Protenase Enzyme from Human Plasma

Degradation of the human proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin by Bacteroides gingivalis

Multiple forms of proteases of Bacteroides gingivalis and their cellular location

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