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Characterization of Bovine Heart Sulfotransferase Catalyzing the Sulfation of Tyrosine-Containing Peptides 00128357 Suiko, Masahito Fernando, P. H. Prasantha 90295197 榊原, 陽一 サカキバラ, ヨウイチ Sakakibara, Yoichi 榊原 サカキバラ Sakakibara 陽一 ヨウイチ Yoichi 宮崎大学 University of Miyazaki Kudo, Hisao 中村, 豊彦 ナカムラ, トヨヒコ Nakamura, Toyohiko 中村 ナカムラ Nakamura 豊彦 トヨヒコ Toyohiko Liu, Ming-Cheh Bovine heart, Sulfotransferase, Tyrosine sulfation Using [35S]PAPS as the sulfate donor, we have detected a sulfotransferase from bovine heart which catalyzes the sulfation of tyrosine-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 stimulated 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 2μM 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. 日本ビタミン学会 1997-08 eng journal article VoR http://hdl.handle.net/10458/1856 https://miyazaki-u.repo.nii.ac.jp/records/460 AA00703822 03014800 Journal of nutritional science and vitaminology J. nutr. sci. vitaminol 43 485 490 https://miyazaki-u.repo.nii.ac.jp/record/460/files/JNSV43.pdf application/pdf 1.0 MB 2020-06-21