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PMID: 6198282 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Infection and immunity ·Vol. 43 ·No. 2 ·1984-02-00 ·Pages 644-8

Carlsson J, Herrmann BF, Höfling JF, Sundqvist GK

Abstract

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.

MeSH Terms
Bacteroides/metabolism Electrophoresis, Polyacrylamide Gel Humans Immunoelectrophoresis Trypsin/metabolism alpha 1-Antitrypsin/metabolism alpha-Macroglobulins/metabolism
Chemicals
alpha 1-Antitrypsin alpha-Macroglobulins Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Carlsson J
Herrmann B F
Höfling J F
Sundqvist G K
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.43.2.644-648.1984
Published
1984-02-00
Pages
644-8
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC264348
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.43.2.644-648.1984 PMC Full Text View journal details
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