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| 2. |
- Christensen, P, et al.
(författare)
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Demonstration of the non-identity between the Fc receptor for human IgG from group A streptococci type 15 and M protein, peptidoglycan and the group specific carbohydrate
- 1979
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Ingår i: Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology. - 0304-1328. ; 87C:3, s. 61-257
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Tidskriftsartikel (refereegranskat)abstract
- After electrophoresis of an alkaline extract of type 15 group A streptococci, three main precipitation lines were obtained in diffusion experiments against commercial human polyclonal IgG (lines 1, 2 and 3). Nineteen of 23 sera (83%) from apparently healthy human individuals gave line 3, while 6 of them (26%) gave line 1. The sera giving line 1 did also give line 3. Line 2 was obtained with 2 sera only, also giving lines 1 and 3. Line 3 was caused by a streptococcal Fc-receptor for human IgG, since the line could be displaced by addition of Fc-fragments, but not Fab-fragments of pooled human IgG. Line 1 was shown to be different from line 3, since (1) line 1 was suppressed in contrast to line 3 on absorption of a human serum or commercial polyclonal human IgG with S. aureus; and (2), line 1 was suppressed by Fab-fragments but not Fc-fragments of polyclonal human IgG. Line 2 could be inhibited by addition of peptidoglycan to commercial polyclonal human IgG or a human serum investigated. Another line, 4, obtained in diffusion experiments involving electrophoretically separated alkaline extract of type 15 group A streptococci was type-specific as shown by rabbit antisera to streptococci type M1, M8, M15, and T44, and disappeared on trypsinization of the extract. The component responsible for line 4 in the streptococcal extract, judged to be type-specific M protein, had a mobility different from the component responsible for line 3 in electrophoresis.
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| 3. |
- Christensen, P, et al.
(författare)
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Interaction of the Fc part of IgG with Lancefield extracts of hemolytic streptococci. Strain specificity and activity
- 1979
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Ingår i: Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology. - 0304-1328. ; 87C:1, s. 7-73
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Tidskriftsartikel (refereegranskat)abstract
- Lancefield extracts of 19 types of group A streptococci as well as one group C and one group G strain were examined for agglutination of human red cells coated with various anti-Rh antibodies. Fourteen extracts agglutinated one or more of the coated cell samples, while five did not. The agglutination was inhibited by Fc but not by Fab fragments of human IgG. After mouse passages, three of the non-agglutinating strains acquired agglutinating capacity. At least three different reactivities were distinguished by the action of the extracts on IgG1 and IgG3 coated cells, respectively. Two of the streptococcal extracts, agglutinating the same anti-Rh coated cells, could be further differentiated in hemagglutination inhibition (HAI) experiments using purified IgG3 myeloma proteins. Five selected agglutinating systems were inhibited by purified myeloma proteins of the IgG1, IgG2, and IgG4 subclasses. IgG3 proteins inhibited only two of the five HAI systems.
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| 4. |
- Eriksson, Caj, et al.
(författare)
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Denatured hemoproteins as catalysts in lipid oxidation
- 1971
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Ingår i: Journal of the American Oil Chemists Society. - 0003-021X .- 1558-9331. ; 48:9, s. 442-447
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Tidskriftsartikel (refereegranskat)abstract
- Purified catalase and peroxidase were denatured by heat, acid and urea. Denaturation resulted in up to 22-fold increase in nonenzymatic lipid oxidation activity concomitant with loss of enzymatic activity. It is proposed that the increased nonenzymatic activity is due to increased exposure of the heme group. Acid-splitting of the hemoproteins into apoprotein and hemin had the greatest influence on both of the catalytic activities and recombination reversed the effect. Urea-denatured hemoprotein possessed increased nonenzymatic activity due to increased exposure of the protein-bound heme, however, peroxidase increased less than catalase which is consistent with the fact that peroxidase is the more heat stable enzyme. Nonenzymatic activity of the heat denatured hemoproteins was maximum when catalase was treated at 90 C for 2 min and peroxidase at 100 to 125 C for 5 to 30 min. © 1971 AOCS.
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| 6. |
- Eriksson, Caj, et al.
(författare)
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Oxidation of fatty acids by heat treated hemoproteins
- 1970
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Ingår i: Lipids. - 0024-4201 .- 1558-9307. ; 5:3, s. 365-366
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Tidskriftsartikel (refereegranskat)abstract
- The hemoproteins catalase and peroxidase, after heat treatment which decreased their enzyme activities, became more efficient as heme catalysts of linoleic acid oxidation. These effects might be of importance for preservation and storage of food. © 1969 American Oil Chemists' Society.
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