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Purification of Rat Pineal Hydroxyindole‐O‐Methyltransferase Using S‐Adenosyl‐L‐Homocysteine Agarose Chromatography
Author(s) -
Sugden David,
Voisin Pierre,
Klein David C.
Publication year - 1986
Publication title -
journal of pineal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.881
H-Index - 131
eISSN - 1600-079X
pISSN - 0742-3098
DOI - 10.1111/j.1600-079x.1986.tb00761.x
Subject(s) - affinity chromatography , agarose , biochemistry , methyltransferase , chromatography , enzyme , chemistry , microbiology and biotechnology , biology , methylation , dna
Rat pineal hydroxyindole‐O‐methyltransferase (HIOMT; EC 2.1.1.4) was purified by affinity Chromatography using an S‐adenosyl‐L‐homocysteine agarose column. This single‐step procedure, which is rapid, simple, and applicable to small quantities of tissue, gave a large enrichment of a protein (M r ∼ 38,000) identified by SDS‐PAGE and silver staining. The amino acid composition of rat HIOMT was generally similar to that of the bovine enzyme, although some differences were apparent. This method will be valuable in isolating sufficient rat HIOMT to enable its primary amino acid sequence to be determined.