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KMID : 0385219970070020058
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Korean Journal of Gerontology
1997 Volume.7 No. 2 p.58 ~ p.63
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Yang Ryung
Yu Je-Wuk
Shin Dong-Bum
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Abstract
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Putative taurine synthesis enzyme, cysteinesulfinate decarboxylase was purified from porcine liver and concentrated by approximatively 200-fold. The molecular weight of the purified enzyme was estimated to be 100,600 dalton and the enzyme was constituted of two subunits whose molecular weights are 48,000 dalton. The cysteinesulfinate decarboxylase was pyridoxal 5’-phosphate dependent enzyme and Km value for cysteinesulfinate was 1.12 mM. The optimum condition for cysteinesulfinate decarboxylase activity was pH7.5 and 40∼45℃. Hypotaurine and taurine did not inhibit the enzyme activity. However, thiol compounds such as dithiothreitol and β-mercaptoethanol were able to activate cysteinesulfinate decarboxylase.
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KEYWORD
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Porcine liver, Cysteinesulfinate decarboxylase, Hypotaurine, taurine
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