1. Treatment of cell-suspension cultures of bean (Phaseolus vulguris cv. Canadian Wonder) with an elicitor preparation heat-released from the cell walls of the phytopathogenic fungus Colletotrichum lindemuthianum resulted in rapid changes in the activities of two microsomal oxygenases, cinnamic acid 4-hydroxylase7 involved in accumulation of wall-bound phenolics and phytoalexins, and proline 2-oxoglutarate dioxygenase (prolyl hydroxylase) involved in the post-translational modification of hydroxyproline-rich glycoproteins.2. An anti-(cytochrome P-450) monoclonal antibody, originally raised against rat cytochrome P-450 isoform c, has been shown to bind to bean microsomes and recognise in Western blots an M,-48000 polypeptide, which comigrates with a haeme-containing protein on SDS/polyacrylamide gel analysis and which has been tentatively identified as a cytochrome P-450 capable of the hydroxylation of cinnamic acid.3. A preparation of proline 2-oxoglutarate dioxygenase purified to homogeneity was used to immunise rabbits for the production of antiserum. An elicitor-induced polypeptide of MI 65000 was identified as prolyl hydroxylase while an antigenically related polypeptide of M I 60000 was also immunoprecipitated but not induced by elicitor treatment.4. Use of the two antibodies has demonstrated rapid transient increases in the synthesis of the M , 48000 and M I 65000 oxygenases in vivo and for mRNAs as measured in in vitro translations, particularly for the putative cytochrome P-450. These increases slightly precede corresponding changes in the synthesis of the soluble enzyme phenylalanine ammonia-lyase, in common with which these oxygenases probably share a mechanism of gene activation underlying the increased activities seen in response to elicitor treatment.Plant endomembrane systems mediate the synthesis, modification and export of wall-bound materials. Among these functions, synthesis of matrix polysaccharides, posttranslational modification and glycosylation of proteins and aromatic hydroxylation of phenolic precursors have particularly been identified. Modulation of activities involved in a number of these processes has been described in endomembranes isolated from cell-suspension cultures of dwarf French bean (Phaseolus vulguris L.) exposed to an elicitor preparation from the cell walls of the phytopathogenic fungus Colletotrichum lindemuthiunum. Prominent among these are two oxygenase activities, the cytochrome-P-450-dependent hydroxylation of cinnamic acid involved in the production of phenylpropanoid precursors of antifungal isoflavonoid phytoalexins and wall-bound phenolic compounds [I -31, and the hydroxylation of peptide proline during the post-translational modification of arabinosylated-hydroxyproline-rich glycoprotein and extensin, both of which are induced in response to elicitor treatment [3,4].