Abstract
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1.
By column chromatography on DEAE-cellulose calcium phosphate mixed gel red cell catalase can be separated in two fractions, 0.15 M saline and 0.15 M secondary phosphate being used as eluants.
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2.
The fractions obtained from blood of normal subjects and of homozygous acatalasia cases differ in electrophoretic mobility and in heat stability. Of the fractions isolated from blood of heterozygous cases, one resembles electrophoretically the normal and the other the acatalatic enzyme.
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3.
The observation that the enzyme fractions isolated from acatalatic blood are less stable and are mainly localized in reticulocytes, suggests, that in acatalasia a labile enzyme variant is synthesized. Therefore, acatalasia may be considered as an enzyme defect due to a structural gene mutation.
Zusammenfassung
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1.
Unter Verwendung eines Gemisches von DEAE-Cellulose-Calciumphosphat-Gel, läßt sich Erythrocytenkatalase in zwei Fraktionen trennen, wobei sich eine durch 0.15 M NaCl, die andere durch 0,15 M sekundäres Phosphat eluieren läßt.
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2.
Die aus Blut normaler Versuchspersonen und homozygoter Akatalasiefälle dargestellten Fraktionen unterscheiden sich hinsichtlich elektrophoretischer Beweglichkeit und Hitzestabilität. Von den beiden aus Blut heterozygoter Defektträger isolierten Fraktionen verhält sich die eine wie die Fraktionen aus normalem Blut, die andere wie diejenigen aus Akatalasieblut.
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3.
Der Befund, daß das aus Akatalasieblut isolierte Enzym relativ unbeständig ist und dieses vor allem in den Reticulocyten vorkommt, berechtigt zur Annahme einer labilen Enzymvariante. Es scheint sich demnach bei den hier untersuchten Fällen von Akatalasie um die Mutation eines Strukturgens zu handeln.
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This is contribution No. 3 of a series of papers on acatalasia published in this journal [1,2].
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Matsubara, S., Suter, H. & Aebi, H. Fractionation of erythrocyte catalase from normal, hypocatalatic and acatalatic humans. Hum Genet 4, 29–41 (1967). https://doi.org/10.1007/BF00279177
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DOI: https://doi.org/10.1007/BF00279177