On the enzymatic hydrolysis of the sulfate conjugate of 3-methoxy-4-hydroxyphenylglycol (MHPG)
The hydrolysis of 3-methoxy-4-hydroxyphenylglycol sulfate conjugate (MHPG-SO 4) by three enzyme preparations (crude sulfatase, pure sulfatase, and glucuronidase) was evaluated. The stability of free MHPG and MHPG-SO 4 to incubation with and without the above enzyme preparation was also assessed. Fro...
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Veröffentlicht in: | Biochemical medicine 1980-12, Vol.24 (3), p.314-320 |
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Sprache: | eng |
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Zusammenfassung: | The hydrolysis of 3-methoxy-4-hydroxyphenylglycol sulfate conjugate (MHPG-SO
4) by three enzyme preparations (crude sulfatase, pure sulfatase, and glucuronidase) was evaluated. The stability of free MHPG and MHPG-SO
4 to incubation with and without the above enzyme preparation was also assessed.
From the results obtained, we concluded that free MHPG is subjected to very little or no decomposition during overnight incubation. The enzyme in the crude sulfatase from Helix Pomatia was found to be superior when compared to the pure sulfatase. It was further determined that 500 units of sulfatase of this enzyme preparation can completely hydrolyze 1 μg MHPG equivalent of MHPG-SO
4 within 1 hr at 40°C or overnight at −10°C. The usefulness of this latter unusual property is discussed. |
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ISSN: | 0006-2944 1557-7996 |
DOI: | 10.1016/0006-2944(80)90025-3 |