A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase
Human cupro‐zinc superoxide dismutase is polymorphic in northern Sweden. The genetic variant type has a lower mobility at electrophoresis in alkaline buffer. The enzyme was isolated from erythrocytes from one of the rare homozygotes and its properties compared to those of the common type. The isoele...
Published in: | European Journal of Biochemistry |
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crwiley:10.1111/j.1432-1033.1976.tb10356.x 2024-06-02T08:12:11+00:00 A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase MARKLUND, Stefan BECKMAN, Gunhild STIGBRAND, Torgny 1976 http://dx.doi.org/10.1111/j.1432-1033.1976.tb10356.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1976.tb10356.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1976.tb10356.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 65, issue 2, page 415-422 ISSN 0014-2956 1432-1033 journal-article 1976 crwiley https://doi.org/10.1111/j.1432-1033.1976.tb10356.x 2024-05-03T11:53:48Z Human cupro‐zinc superoxide dismutase is polymorphic in northern Sweden. The genetic variant type has a lower mobility at electrophoresis in alkaline buffer. The enzyme was isolated from erythrocytes from one of the rare homozygotes and its properties compared to those of the common type. The isoelectric point of the variant was higher (4.85) than that of the common type (4.7). Small differences in amino acid composition were found but no definite amino acid substitutions could be pointed out. The molecular weights were equal as judged from electrophoreses in polyacrylamide gels in the presence of dodecylsulphate. The ultraviolet spectra were similar. Parameters related to the active site of the enzyme were very similar; i.e. specific activity and sensitivity to inhibition by cyanide and by H 2 O 2 . These parameters, especially the latter two, differ widely between species. Both enzymes were stable for weeks at neutral pH at 37 °C, whereas the common type was significantly more stable at pH 4 and pH 11 and also at incubation in neutral buffer at 70 °C. It appears that the active site of the variant is conserved whereas the stability of the enzyme is affected. Article in Journal/Newspaper Northern Sweden Wiley Online Library European Journal of Biochemistry 65 2 415 422 |
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English |
description |
Human cupro‐zinc superoxide dismutase is polymorphic in northern Sweden. The genetic variant type has a lower mobility at electrophoresis in alkaline buffer. The enzyme was isolated from erythrocytes from one of the rare homozygotes and its properties compared to those of the common type. The isoelectric point of the variant was higher (4.85) than that of the common type (4.7). Small differences in amino acid composition were found but no definite amino acid substitutions could be pointed out. The molecular weights were equal as judged from electrophoreses in polyacrylamide gels in the presence of dodecylsulphate. The ultraviolet spectra were similar. Parameters related to the active site of the enzyme were very similar; i.e. specific activity and sensitivity to inhibition by cyanide and by H 2 O 2 . These parameters, especially the latter two, differ widely between species. Both enzymes were stable for weeks at neutral pH at 37 °C, whereas the common type was significantly more stable at pH 4 and pH 11 and also at incubation in neutral buffer at 70 °C. It appears that the active site of the variant is conserved whereas the stability of the enzyme is affected. |
format |
Article in Journal/Newspaper |
author |
MARKLUND, Stefan BECKMAN, Gunhild STIGBRAND, Torgny |
spellingShingle |
MARKLUND, Stefan BECKMAN, Gunhild STIGBRAND, Torgny A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase |
author_facet |
MARKLUND, Stefan BECKMAN, Gunhild STIGBRAND, Torgny |
author_sort |
MARKLUND, Stefan |
title |
A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase |
title_short |
A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase |
title_full |
A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase |
title_fullStr |
A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase |
title_full_unstemmed |
A Comparison between the Common Type and a Rare Genetic Variant of Human Cupro‐Zinc Superoxide Dismutase |
title_sort |
comparison between the common type and a rare genetic variant of human cupro‐zinc superoxide dismutase |
publisher |
Wiley |
publishDate |
1976 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1976.tb10356.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1976.tb10356.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1976.tb10356.x |
genre |
Northern Sweden |
genre_facet |
Northern Sweden |
op_source |
European Journal of Biochemistry volume 65, issue 2, page 415-422 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1976.tb10356.x |
container_title |
European Journal of Biochemistry |
container_volume |
65 |
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2 |
container_start_page |
415 |
op_container_end_page |
422 |
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1800758539898060800 |