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PURIFICATION AND CHARACTERIZATION OF A MICROBIAL XANTHINE DEHYDROGENASE HIGHLY ACTIVE TOWARDS HXPOXANTHINE
Kim, Jong Min Schmid, Rolf D.
Kim, Jong Min
Schmid, Rolf D.
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Issue Date
1989
Submitted date
2024-01-16
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Abstract
We purified xanthine dehydrogenase (EC 1.2.1.37) from Pseudomonas putida Fl, which was screened with hypoxanthine as the main carbon and nitrogen source. The purified enzyme was homogeneous judged by polyacrylamide gel electrophoresis with or without SDS and HPLC on a TSK G-3000 SW column. The enzyme showed an absorption maximum at 457 nm in the visible range and shoulders between 300 to 400 mm and 500 and 600 rm. The absorption ratio at 280 nm to 450 mm was 5.9. The enzyme showed higher activity with hypoxanthine than xanthine as substrate with NADt as an effective electron acceptor. Purine was a poor substrate and neither adenine nor guanine was oxidized by the enzyme. Specific activity was 80.2 U/mg with hypoxanthine as substrate, and Kn values for hypoxanthine, xanthine and NAD‘ were 40, 64 and 52 UM, respectively. The molecular weight of the native enzyme was estimated to be 350,000 by HPLC on a TSK G- 3000 SW column, and those of two different subunits were 92,000 and 46,000 by SDSpolyacrylamide gel electrophoresis, respectively. Other catalytic properties of the enzyme were also reported.
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Biosensors : applications in medicine, environmental protection and process control, 421 - 424
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Book chapter
conference paper
conference paper
Language
en
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GBF monographs ; Volume 13
ISSN
0930-4320
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ISBN
3527280324
0895739550
0895739550
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Attribution-NonCommercial-ShareAlike 4.0 International