Characterization of Bovine Heart Sulfotransferase Catalyzing the Sulfation of Tyrosine-Containing Peptides.
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- SUIKO Masahito
- Department of Biological Resource Science, Miyazaki University
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- FERNANDO P. H. Prasantha
- Department of Biological Resource Science, Miyazaki University
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- SAKAKIBARA Yoichi
- Department of Biological Resource Science, Miyazaki University
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- KUDO Hisao
- Department of Biological Resource Science, Miyazaki University
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- NAKAMURA Toyohiko
- Department of Biological Resource Science, Miyazaki University
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- LIU Ming-Cheh
- Department of Biochemistry, The University of Texas Health Center at Tyler
Bibliographic Information
- Other Title
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- Characterization of Bovine Heart Sulfot
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Abstract
Using [35S] PAPS as the sulfate donor, we have detected a sulfotransferase from bovine heart which catalyzes the sulfation of tyro-sine-containing peptides. The enzyme displayed optimal activity at pH 5.75 and 35°C in a one-hour reaction. The addition of 10 mM Mn2+ or Co2+ to the reaction mixture increased the sulfotransferase activity by 3.4-and 3.5-fold, respectively. In contrast, the maximum increment stimu-lated by Mg2+ was only 1.75-fold at 15 mM concentration, and instead of exerting an enhancement effect, Ca2+ was found to be a potent inhibitor. The addition of 50 mM NaF to the reaction mixture resulted in an increase in sulfotransferase activity of 3.3-fold. The Km for 3'-phosphoadenosine 5'-phosphosulfate (PAPS) was determined to be 2 μM at a constant 0.5 mM Boc-Glu-Asp-Tyr-Val. Among the 10 peptides tested as substrates, Boc-Glu-Asp-Tyr-Val and Boc-Asp-Asp-Tyr-Val provided the highest activities.
Journal
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- Journal of Nutritional Science and Vitaminology
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Journal of Nutritional Science and Vitaminology 43 (4), 485-490, 1997
Center for Academic Publications Japan
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Details 詳細情報について
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- CRID
- 1390001206321003264
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- NII Article ID
- 130001370330
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- NII Book ID
- AA00703822
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- ISSN
- 18817742
- 03014800
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- HANDLE
- 10458/1856
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- NDL BIB ID
- 4287794
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- PubMed
- 9328868
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed