| 1. |
- Berglund, Björn E., et al.
(författare)
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Late Weichselian environmental change in southern Sweden and Denmark
- 1994
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Ingår i: Journal of Quaternary Science. - : Wiley. - 0267-8179 .- 1099-1417. ; 9:2, s. 127-132
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Tidskriftsartikel (refereegranskat)abstract
- A synthesis is presented of the envronmental and climatic variations that are inferred to have occurred in southern Sweden (up to latitude 59°N) and Denmark during the Weichselian Late-glacial (14-9 ka BP). The chronology and characteristics of the main phases of deglaciation, sea-level change, periglacial activity, soil development, vegetation cover and climate change are summarised. A curve representing the main changes in temperature, including quantitative estimates based upon beetle data and using the ‘mutual climatic range’ method, is presented.
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| 3. |
- De Château, M, et al.
(författare)
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On the interaction between protein L and immunoglobulins of various mammalian species
- 1993
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Ingår i: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 37:4, s. 399-405
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Tidskriftsartikel (refereegranskat)abstract
- Protein L, a cell wall molecule of certain strains of the anaerobic bacterial species Peptostreptococcus magnus, shows high affinity for human immunoglobulin (Ig) light chains. In the present study protein L was tested against a panel of human myeloma proteins of the IgG, IgM, IgA and IgE classes, and strong binding was seen with antibodies carrying kappa light chains. A high degree of specificity for Ig was demonstrated in binding experiments with human plasma proteins. Apart from human Ig, strong protein L-binding activity was also detected in the serum of 12 out of 23 tested additional mammalian species, including other primates and rodents. Subsequent analysis with purified Ig samples demonstrated the binding of protein L to Ig of important laboratory animal species such as the mouse, the rat and the rabbit. The affinity constants for the interactions between protein L and polyclonal IgG of these species were 2.6 x 10(9), 3.9 x 10(8) and 7.4 x 10(7), respectively. In non-human species, the binding of protein L was also found to be mediated through Ig light chains, and the results demonstrate the potential value of protein L as an immunochemical tool.
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