Apparent identity of cerebral tyrosylsulfotransferase activities using either a cholecystokinin derivative or an acidic amino acid polymer as substrate.
The tyrosylsulfotransferase activities of rat cerebral fractions transferring [35S]sulfate groups from 3'-phosphoadenosine 5'-[35S]phosphosulfate to either Boc-cholecystokinin-8 (in non-sulfated form) or the acidic amino acid polymer (Glu, Ala, Tyr)n (6:3:1) were compared. They appear similar regarding subcellular distribution (both being enriched in the microsomal fraction) and inhibition by an excess of the acidic amino acid polymer, NaCl or 2,6-dichloro 4-nitrophenol. These results obtained with artificial substrates suggest that identical (or closely similar) tyrosylsulfotransferases are responsible for sulfation of tyrosine residues of several secretory proteins from various tissues.
Vargas
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F
Schwartz
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JC
D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002766:Cholecystokinin / Q000031:analogs & derivatives*; D008297:Male; D008861:Microsomes / Q000201:enzymology; D009596:Nitrophenols / Q000494:pharmacology; D011108:Polymers; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology; D015238:Sulfotransferases; D013466:Sulfurtransferases / Q000378:metabolism*
D000596:Amino Acids; D009596:Nitrophenols; D011108:Polymers; C015802:2,6-dichloro-4-nitrophenol; D002766:Cholecystokinin; D013466:Sulfurtransferases; D015238:Sulfotransferases; C039079:protein-tyrosine sulfotransferase