論文 - 榊原 陽一
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Manganese-dependent dopa/tyrosine sulfation in HepG2 human hepatoma cells: novel dopa/tyrosine sulfotransferase activities associated with the human monoamine-form phenol sulfotransferase
Sakakibara, Y., Katafuchi, J.Takami, Y., Nakayama, T.その他２名
BiochimicaBiophysicaActaVol. 1355, No. 2102-106 1997年2月
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Suiko Masahito, Fernando P.H.Prasantha, Sakakibara Yoichi, KUDO Hisao, NAKAMURA Toyohiko, LIU Ming-Cheh
Journal of Nutritional Science and Vitaminology 43 ( 4 ) 485 - 490 1997年
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：日本ビタミン学会
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.
DOI： 10.3177/jnsv.43.485
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Suiko M., Suiko M., Sakakibara Y., Sakakibara Y., Nakajima H., Sakaida H., Sakaida H., Liu M.
Biochemical Journal 314 ( 1 ) 151 - 158 1996年2月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Biochemical Journal
HepG2 human hepatoma cells, labelled with [35S]sulphate in media containing L-3,4-dihydroxyphenylalanine (L-dopa), (D-dopa), DL-m-tyrosine or D-p-tyrosine, were found to produce the [35S]sulphated forms of these compounds. Addition to the labelling media of m-hydroxybenzylhydrazine, an aromatic amino acid decarboxylase inhibitor, greatly enhanced the production of L-dopa O-[35S]sulphate and DL-m-tyrosine O-[35S]sulphate, with a concomitant decrease in the formation of dopamine O-[35S]sulphate and m-tyramine O-[35S]sulphate. With 3′-phosphoadenosine 5′-phospho[35S]sulphate as the sulphate donor, HepG2-cell cytosol was shown to contain enzymic activity catalysing the sulphation of L-dopa, D-dopa, L-m-tyrosine, D-m-tyrosine, L-p-tyrosine and D-p-tyrosine. The pH optimum of the enzyme, designated dopa/tyrosine sulphotransferase, was determined to be 8.75 with D-m-tyrosine as the substrate. The enzyme exhibited stereoselectivity for the D-form of dopa or tyrosine isomers. Addition of 10 mM MnCl2 to the reaction mixture resulted in a remarkable stimulation of dopa/tyrosine sulphotransferase activity, being as high as 267.8 times with D-p-tyrosine as the substrate. Quantitative assays revealed L-dopa, D-dopa and D-m-tyrosine to be better substrates than L-p-tyrosine. When the HepG2-cell cytosol was subjected to DEAE Bio-Gel and hydroxyapatite column chromatography, dopa/tyrosine sulphotransferase was co-eluted with the thermolabile 'M-form' phenol sulphotransferase. Furthermore dopa/tyrosine sulphotransferase displayed properties similar to that of the M-form phenol sulphotransferase with respect to thermostability and sensitivity to 2,6-dichloro-4-nitrophenol. Whether the M-form phenol sulphotransferase is truly (solely) responsible for the dopa/tyrosine sulphotransferase activity present in HepG2 cells remains to be clarified.
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Enzymic sulphation of dopa and tyrosine isomers by HepG2 human hepatoma cells: stereoselectivity and stimulationby Mn2+
Suiko, M., Sakakibara, Y., Nakajima, H.Sakaida, H., Liu, M.-C.
Biochemical JournalVol. 314, No. 1151-158 1996年2月
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Desulfation of tyrosine-O-sulfated peptides by some eukaryotic sulfatases
Suiko, M., Tojo, T., Fern o, P.H.P.Sakakibara, Y.その他２名
BioscienceBiotechnologyBiochemistryVol. 60, No. 1137-138 1996年1月
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Purification, characterization, and molecular cloning of a novel rat liver dopa/tyrosine sulfotransferase
Sakakibara, Y., Takami, Y., Zwieb, C.Nakayama, T.その他３名
The Journal of Biological ChemistryVol. 270, No. 5130470-30478 1995年12月
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Sulfation of L-tyrosine in mammalian cells: a comparative study
Sakakibara, Y., Suiko, M., Nakajima, H., Liu, M.-C.
Biochemical JournalVol. 305, No. 3993-998 1995年2月
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Sulfation of L-tyrosine in higher plants and mammalian animals
Suiko, M., Sakakibara, Y.
Proceeding of IPBARogla, Slovenia211-222 1994年12月
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De novo sulfation of L-tyrosine in HepG2 human hepatoma cells and its possible functional implication
Sakakibara, Y., Suiko, M., Liu, M.-C.
European Journalof BiochemistryVol. 226, No. 2293-301 1994年12月
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Purification and characterization of two molecular forms of bovine complement factor H
Sakakibara, Y., Suiko, M.Fern o, P.H.P., Miura, M., Liu, M.-C.
Animal CellTechnology: Basic & Applied AspectsVol. 6581-588 1994年8月
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Sakakibara Y., Sakakibara Y., Suiko M., Fernando P., Ohashi T., Liu M.
Cytotechnology 14 ( 2 ) 97 - 107 1994年1月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Cytotechnology
A major tyrosine-O-sulfate (TyrS)-binding protein present in bovine serum was purified to electrophoretic homogeneity using a combination of TyrS-Affi-Gel 10 affinity chromatographyy, DEAE-Bio-Gel A ion-exchange chromatography, and hydroxylapatite chromatography. The purified TyrS-binding protein migrated as doublet protein bands with apparent molecular weights of ca. 160, 000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. N-termini of the two forms of purified TyrS-binding protein contain most likely identical sequence for the first fifteen amino acids residues, which displays a high degree of homology to those of human and mouse complement factor H. Furthermore, the purified TyrS-binding protein exhibited immunologic cross-reactivity with anti-human complement factor H. These results indicate the identity of the purified TyrS-binding protein being bovine complement factor H. The two forms of the purified bovine factor H were investigated with respect to the sensitivity to limited trypsin digestion. The high-molecular weight form was cleaved into two fragments with apparent molecular masses of, respectively, 45 kD and 125 kD. The low-molecular weight form was cleaved in a different manner to generate three major fragments with molecular masses of 25 kD, 45 kD and 100 kD, respectively. Limited V8 protease mapping of the two forms yielded similar, yet unidentical, peptide band patterns. Purified bovine factor H appeared to bind agarose-bonded heparin through its anion-binding domain and the binding was inhibited by the presence of free heparin or dextran sulfate. © 1994 Kluwer Academic Publishers.
DOI： 10.1007/BF00758174
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Preparation of 3’-phosphoadenosine 5’-phospho35S-sulfate using ATP sulfurylase and APS kinase from Bacillus stearothermophilus: enzymatic synthesis and purification
Fern o, P.H.P., Karakawa, A.Sakakibara, Y., Ibuki, H. その他3名
Bioscience,Biotechnologyand BiochemistryVol. 57, No. 111974-1975 1993年11月
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Isolation and characterization of a novel microsomal membrane-bound phenol sulfotransferase from bovine liver
Fern o, P.H.P., Sakakibara, Y.Nakatsu, S., Suiko, M. その他2名
Biochemistryand MolecularBiologyInternationalVol. 30, No. 3433-441 1993年3月
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Suiko M., Fernando P., Sakakibara Y., Nakajima H., Liu M., Abe S., Nakatsu S.
Nucleic acids symposium series ( 27 ) 183 - 184 1992年12月
記述言語：英語 掲載種別：研究論文（学術雑誌） 出版者・発行元：Nucleic acids symposium series
In vitro tyrosine sulfation of recombinant proteins would be a valuable tool in converting those proteins expressed in prokaryotic vectors to their natural form. For this purpose tyrosylprotein sulfotransferase (TPST), the enzyme responsible for tyrosine sulfation of proteins, was characterized from a bovine liver Golgi preparation. TPST was active in a acidic environment with a pH optimum of 6.25, and displayed a stimulation by the Mn2+, with the optimum activity in the presence of 5mM MnCl2. TPST was able to sulfate recombinant hirudin variant 1 (rHV-1) expressed in Escherichia coli and the C-terminal hirudin fragment 54-65 but not the N-terminal hirudin fragment 1-15 by using 3'-phosphoadenosine 5'-phosphosulfate (PAPS), indicating its specificity for the naturally sulfated tyrosine 63. Comparison of the reaction kinetics on synthetic peptides showed that the bovine liver TPST has a higher affinity and reaction rates for those peptides with a aspartyl residue on the N-terminal side of the tyrosine when compared with a glutamyl residue.
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Detoxication of phenolic xenobiotics in microsomal membranes: a novel phenol sulfotransferase activity in bovine liver microsomes
Suiko, M., Fern o, P.H.P.Sakakibara, Y., Liu, M.-C.
Proceeding of the6th China-Japan Symposiumon PesticideScience,Fukuoka, Japan151-155 1992年11月
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Protein tyrosine sulfation in animal cells and its simulation in vitro in the downstream processing of proteins
Fern o, P.H.P., Sakakibara, Y.Abe, S., Liu, M.-C. その他２名
Animal Cell Technology: Basic & Applied AspectsVol. 4473-479 1992年8月