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KMID : 0364219900330040468
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Korean Journal of Zoology
1990 Volume.33 No. 4 p.468 ~ p.475
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Further Characterization of Protein Sulfotransferase(s) of Rat Brain by Alkaline Hydrolysis of Sulfated Proteins
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Ryu Jae-Wook
Choi Myung-Un
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Abstract
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An In vitro protein sulfation in the soluble fraction of rat brain was charaderized further by an improved method of alkaline hydrolysis and thin layer ceflulose electrophoresis TLE) The protein sulfation was carried out in a reaction system containing [35 S] 3'-phosphoadenosine-5'-phosphosulfate (PAPS), Tris-maleate buffer (pH 8), MgCI2, and soluble proteins from rat brain. The sulfated proteins were precipitated by acetone and alkaline hydrolysis was performed to obtain sulfated amino acids. The hydrolysate was separated further by TLE and the separated residues were identified by fluorography. The Iluorography of one-dimensional The showed at least nine sulfated residues including tryosine-O-sulfate. The other spots were not identified yet positively. General properties of protein sulfotransferases (PST) using this method were re-examined such as effects of concentrations of PAPS, pH, incubation temperature and Mg2+. These results suggest a possible occurrence of several PST corresponding to each sulfated residue in rat brain and that the sulfation can occur not only in tyrosine but also in other residues as well.
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KEYWORD
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Protein sulfotransferases, Protein sulfation, Sulfated amino acid, Tyrosine-O-sulfate, Alkaline hydrolysis of protein
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