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Preparation of the lactate oxidase apoenzyme and studies on the binding of flavin mononucleotide to the apoenzyme

Y S Choong, M G Shepherd, P A Sullivan
Biochemical Journal Jan 01, 1975, 145 (1) 37-45; DOI: 10.1042/bj1450037
Y S Choong
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M G Shepherd
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P A Sullivan
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Abstract

1. Lactate oxidase from Mycobacterium smegmatis is completely resolved into free flavin and apoenzyme by treatment with acid (NH4)2SO4. 2. Reconstitution involves rapid binding of FMN, but the recovery of enzyme activity was slower and appeared to be biphasic. 3. The preparation of the holoenzyme obtained differs from the native enzyme in specific activity, extinction coefficients and mobility on disc-gel electrophoresis. 4. Dialysis of this reconstituted enzyme in 0.1 M-sodium phosphate buffer, pH 7.0, at 0 degrees C for 1 week yields a preparation which closely resembles the native enzyme.

  • © 1975 London: The Biochemical Society
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January 1975

Volume: 145 Issue: 1

Biochemical Journal: 145 (1)
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Preparation of the lactate oxidase apoenzyme and studies on the binding of flavin mononucleotide to the apoenzyme
Y S Choong, M G Shepherd, P A Sullivan
Biochemical Journal Jan 1975, 145 (1) 37-45; DOI: 10.1042/bj1450037
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Preparation of the lactate oxidase apoenzyme and studies on the binding of flavin mononucleotide to the apoenzyme
Y S Choong, M G Shepherd, P A Sullivan
Biochemical Journal Jan 1975, 145 (1) 37-45; DOI: 10.1042/bj1450037

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