Abstract:
:Epicotyl and primary leaves of pea seedlings (Pisum sativum L., var. Alaska) were found to contain soluble and microsomal enzymes catalyzing the addition of glutathione to the olefinic double bond of cinnamic acid. Glutathione S-cinnamoyl transfer was also obtained with enzyme preparations from potato slices and cell suspension cultures of parsley and soybean.The pea transferases had pH-optima between pH 7.4 and 7.8 Km-values were 0.1-0.4 mM and 1-4 mM for cinnamic acid and glutathione, respectively. V-values were between 2-15 nmol mg(-1) protein x min.Chromatography on Sephacryl S-200 indicated that the soluble pea glutathione S-cinnamoyl transferase activity existed in molecular weight forms of 37,000, 75,000, and 150,000. The glutathione-dependent cleavage of the herbicide fluorodifen was catalyzed by a different soluble enzyme activity which eluted in molecular weight positions of 47,000 and/or 82,000.The microsomal fraction from pea primary leaves also catalyzed the conjugation of the carcinogen benzo[α]pyrene with glutathione.
journal_name
Plantajournal_title
Plantaauthors
Diesperger H,Sandermann H Jrdoi
10.1007/BF00388845subject
Has Abstractpub_date
1979-10-01 00:00:00pages
643-8issue
5eissn
0032-0935issn
1432-2048journal_volume
146pub_type
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