Abstract
1. 1. The transfer of sulfate ester group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to poly-(Glu 6, Ala 3, Tyr 1 ) (EAY; M r 47 kDa) in rat submandibular salivary gland has been investigated. The highest tyrosylprotein sulfotransferase activity was obtained in the Golgi-enriched fraction in the presence of 2mM 5'AMP, 20 mM MnCl 2 and 50 mM NaF at pH 6.2. 2. 2. The apparent K m values for EAY and PAPS were 1.6 × 10 −6 and 1.9 × 10 −6M, respectively. 3. 3. Inclusion of NaCl, EDTA, NEM and DTT was inhibitory for the enzyme activity. The enzyme was 28 times less susceptible to 2,6-dichloro-4-nitrophenol inhibition than to phenol sulfotransferase inhibition. 4. 4. This study is the first report characterizing a sulfotransferase activity specific for tyrosylprotein in rat submandibular salivary glands.
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