Nickel-content of urease from Bacillus pasteurii (original) (raw)

Abstract

Urease from Bacillus pasteurii DSM 33 was purified 34-fold to a maximum specific activity of 996.5 μmol urea min-1 mg-1 at 30°C. Homogeneity was demonstrated by isoelectric focussing which showed a single protein zone corresponding to a pI of about 4.6. The native enzyme was demonstrated to have a molecular mass of 230000 and to consist of identical subunits of 65 500, as measured by SDS electrophoresis. Radioactive 63Ni-nickel co-chromatographed with urease through gel filtration, ion-exchange, and affinity chromatography. Measuring specific radioactivity, the nickel content was found to be 1.00 (±0.1) g-atom Ni per mol of subunit, and 0.82 g-atom Ni per mol as measured by atomic absorption spectrometry. This indicates that 1 atom of nickel is present in each of four subunits of the enzyme.

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Abbreviations

SDS:

sodium dodecyl sulfate

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  1. Fachrichtung Mikrobiologie der Universität des Saarlandes, Im Stadtwald, D-6600, Saarbrücken, Federal Republic of Germany
    Stefan Christians & Heinrich Kaltwasser

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  1. Stefan Christians
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  2. Heinrich Kaltwasser
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Christians, S., Kaltwasser, H. Nickel-content of urease from Bacillus pasteurii.Arch. Microbiol. 145, 51–55 (1986). https://doi.org/10.1007/BF00413026

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