Abstract
Phenylalanine ammonia-lyase (PAL) activity was demonstrated in extracts of acetone powders of bean hypocotyls. Since it was observed that cinnamic acid was produced with or without added l-phenylalanine, the origin of this cinnamic acid was investigated. Assay of boiled extracts indicated that cinnamic acid production, with or without added substrate, was enzymatic, and it was shown dialyzed extracts produced cinnamic acid only with added substrate. It was found that extracts contained phenylalanine at four times the level necessary to account for cinnamic acid production without added substrate, and the loss of phenylalanine during autolysis was stoichiometrically equivalent to the cinnamic acid produced. Cinnamic acid was not released during acid or alkaline treatment of extracts, but ferulic acid was found from the alkali treatments. No other evidence for the existence of bound forms of cinnamic acid was obtained, and we conclude that measurements of cinnamic acid production is a valid method of assay for PAL in extracts of acetone powders of bean hypocotyls.
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