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- Grubb, A, et al.
(författare)
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Isolation and some properties of an IgG Fc-binding protein from group A streptococci type 15
- 1982
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Ingår i: International Archives of Allergy and Applied Immunology. - : S. Karger AG. - 0020-5915 .- 1018-2438 .- 1423-0097. ; 67:4, s. 76-369
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Tidskriftsartikel (refereegranskat)abstract
- An IgG Fc-binding protein was isolated from alkaline extracts of group A streptococci type 15 by ion-exchange chromatography and immunosorption on an IgG column. Ample use of protease inhibitors was necessary to achieve successful isolation. 600 micrograms protein was obtained from 60 g bacteria (wet weight). The protein appeared homogeneous on agarose gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 29,500. It contained appreciable amounts of the amino acids glutamic acid, alanine, leucine, aspartic acid and lysine, but little or no tyrosine, phenylalanine, proline, glucosamine or galactosamine. It precipitated human monoclonal IgG of all four sub-classes in agarose gels as well as polyclonal IgG, IgG Fc and normal human serum. It did not precipitate IgG Fab, IgA, IgM, IgD or free kappa or lambda chains.
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| 2. |
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| 3. |
- Schalén, C, et al.
(författare)
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Demonstration of separate receptors for human IgA and IgG in group A streptococci type 4. Separation of the solubilized receptors from group- and type-specific antigens, lipoteichoic acid and peptidoglycan
- 1980
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Ingår i: Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology. - : Wiley. - 0304-1328. ; 88:2, s. 77-82
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Tidskriftsartikel (refereegranskat)abstract
- The alkaline extract of group A streptococci type 4 was separated by electrophoresis and diffused against 27 normal human sera. One of the precipitates appeared with 85% of the sear. Addition of purified IgA myeloma protein or sera containing IgA M-components to the extract changed the electrophoretic mobility of the precipitate anodically. Purified IgG Fc-fragments or sera containing IgG M-component did not affect the mobility of the precipitate. It was concluded that this precipitate contained the streptococcal receptor for human IgA. A non-precipitating IgG Fc-receptor, with agglutinating capacity for cells coated with human IgG1 but not IgG3, was localized by preparative electrophoresis to the same electrophoretic region as the IgA receptor. The mobility of the IgG receptor remained unaltered on addition of IgA myeloma protein permitting a separation of the two receptors by preparative electrophoresis. The receptors were distinct from the group specific carbohydrate, peptidoglycan and lipoteicholic acid. No M antigen or opacity factor were demonstrated in the extract.
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| 4. |
- Schalén, Lucyna, et al.
(författare)
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High isolation rate of Branhamella catarrhalis from the nasopharynx in adults with acute laryngitis
- 1980
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Ingår i: Scandinavian Journal of Infectious Diseases. - 1651-1980. ; 12:4, s. 277-280
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Tidskriftsartikel (refereegranskat)abstract
- Branhamella catarrhalis was isolated from the nasopharynx in 55% of 40 noncompromised adult patients suffering from acute laryngitis. Diplococcus pneumoniae and haemophilus influenzae were found in another 5 and 8%, respectively; one patient had group A streptococci in the throat specimen. In 90% of the patients the laryngitis complaints were preceded by symptoms of an acute respiratory tract infection. Two of the patients with B. catarrhalis showed a significant titre conversion against influenza B and parainfluenza type e virus, respectively. Attempts to isolate virus failed in all cases. The results indicate that B. catarrhalis, known to cause acute otitis media in small children and respiratory tract infections in adult compromised hosts, may be involved in the etiology of acute laryngitis in otherwise healthy adults.
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