A rapid nonchromatographic assay for aminopropyltransferases.
Aminopropyltransferases are key enzymes in the biosynthesis of the polyamines spermidine and spermine. A procedure is described for assaying these enzymes by differential charcoal adsorption of 14C-labeled decarboxylated adenosylmethionine substrate from the labeled polyamine product. This assay is linear with time and enzyme concentration, and is suitable for use with a variety of amine acceptors. This procedure has the advantage, over those previously used, that it is extremely rapid yet very sensitive.
D000327:Adsorption; D002606:Charcoal; D011232:Chemical Precipitation; D004926:Escherichia coli / Q000201:enzymology; D011073:Polyamines / Q000096:biosynthesis; D012436:S-Adenosylmethionine / Q000031:analogs & derivatives; D011436:Spermidine Synthase / Q000032:analysis*; D013379:Substrate Specificity; D014166:Transferases / Q000032:analysis*
D011073:Polyamines; D002606:Charcoal; C012702:S-adenosyl-3-methylthiopropylamine; D012436:S-Adenosylmethionine; D014166:Transferases; D011436:Spermidine Synthase