PMID- 8948087 OWN - NLM STAT- MEDLINE DCOM- 19970228 LR - 20061115 IS - 0049-8254 (Print) IS - 0049-8254 (Linking) VI - 26 IP - 11 DP - 1996 Nov TI - Design, production and characterization of antibodies discriminating between the phenol- and monoamine-sulphating forms of human phenol sulphotransferase. PG - 1113-9 AB - 1. Phenol sulphotransferases (PSTs) are important enzymes in xenobiotic and endobiotic detoxication, and a key component of the body's chemical defence mechanism. 2. Human phenol-(P-PST) and monoamine-(M-PST) sulphating forms of PST share 93% amino acid sequence identity, and to date the various antibodies produced against PSTs all recognize both enzymes. 3. We have identified two peptides based on the cDNA-derived amino acid sequences of human P-PST and M-PST, which elicited for the first time antibodies capable of discriminating between these highly homologous enzymes. 4. These antibodies represent valuable tools for studying the expression, distribution and function of human phenol sulphotransferases. FAU - Rubin, G L AU - Rubin GL AD - Department of Biochemical Medicine, University of Dundee, Ninewells Hospital and Medical School, Dundee, UK. FAU - Sharp, S AU - Sharp S FAU - Jones, A L AU - Jones AL FAU - Glatt, H AU - Glatt H FAU - Mills, J A AU - Mills JA FAU - Coughtrie, M W AU - Coughtrie MW LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - England TA - Xenobiotica JT - Xenobiotica; the fate of foreign compounds in biological systems JID - 1306665 RN - 0 (Antibodies) RN - 0 (Peptides) RN - EC 2.8.2.1 (Arylsulfotransferase) SB - IM MH - Amino Acid Sequence MH - Antibodies/*analysis MH - Arylsulfotransferase/immunology/*metabolism MH - Humans MH - Immunoblotting MH - Molecular Sequence Data MH - Peptides/*immunology EDAT- 1996/11/01 00:00 MHDA- 1996/11/01 00:01 CRDT- 1996/11/01 00:00 PHST- 1996/11/01 00:00 [pubmed] PHST- 1996/11/01 00:01 [medline] PHST- 1996/11/01 00:00 [entrez] AID - 10.3109/00498259609050256 [doi] PST - ppublish SO - Xenobiotica. 1996 Nov;26(11):1113-9. doi: 10.3109/00498259609050256.