This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Singh, B. K. Articles by Conn, E. E. Search for Related Content PubMed PubMed Citation Articles by Singh, B. K. Articles by Conn, E. E. Agricola Articles by Singh, B. K. Articles by Conn, E. E.

Articles

Chorismate Mutase Isoenzymes from Selected Plants and Their Immunological Comparison with the Isoenzymes from Sorghum bicolor¹

Department of Biochemistry and Biophysics, University of California, Davis, California 95616

The isoenzyme pattern of chorismate mutase (EC 5.4.99.5) was examined by diethylaminoethyl-cellulose chromatography in a wide variety of plants. All plants contained a regulated form of chorismate mutase (CM-1), and most contained an additional, unregulated form (CM-2). The regulatory properties of CM-1 differed significantly between plants. Antisera prepared against CM-1 and CM-2 from Sorghum bicolor were used to test immunological cross reaction of chorismate mutases from other plants. There was a high degree of similarity between chorismate mutase isoenzymes from Sorghum bicolor and Zea mays and some with Hordeum vulgare, but all other species studied were antigenically distinct from sorghum. No homology between the structure of CM-1 and CM-2 was detected within any species.

This article has been cited by other articles:

				J. G. Dubouzet, A. Ishihara, F. Matsuda, H. Miyagawa, H. Iwata, and K. Wakasa Integrated metabolomic and transcriptomic analyses of high-tryptophan rice expressing a mutant anthranilate synthase alpha subunit J. Exp. Bot., September 4, 2007; (2007) erm179v1. [Abstract] [Full Text] [PDF]