caa a22 4500 477101801 CHVBK 20180405111544.0 cr unu---uuuuu 170330e19960801xx s 000 0 eng 10.1007/BF00195187 doi (NATIONALLICENCE)springer-10.1007/BF00195187 Subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in higher plants: an immunological investigation [Elektronische Daten] [Michael Witty, Russell Jones, Matthew Robb, Peter Shoolingin Jordan, Alison Smith] A recombinant plasmid, pArab8, harbouring the cDNA encoding the mature form of the tetrapyrrole synthesis enzyme porphobilinogen deaminase (EC 4.3.1.8; also known as hydroxymethylbilane synthase) from Arabidopsis thaliana (L.) Heynh. has been constructed, and used to transform Escherichia coli. The porphobilinogen deaminase protein from Arabidopsis was overexpressed in this strain, and purified to homogeneity (3000-fold) with a yield of 20%. Antibodies were raised against the purified plant enzyme, and used in Western blot analysis, immunoprecipitation of enzyme activity and immuno-gold electron microscopy. The results indicate that the enzyme is confined to plastids in both leaves and roots. The implications of this finding for plant tetrapyrrole synthesis are discussed. Springer-Verlag, 1996 Arabidopsis nationallicence Chlorophyll biosynthesis nationallicence Plastid nationallicence Porphobilinogen deaminase (purification, subcellular location) nationallicence DEAE : diethylaminoethyl nationallicence FPLC : fast protein liquid chromatography nationallicence PBG : porphobilinogen nationallicence Witty Michael Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK aut Jones Russell Toxicology Unit, MRC Laboratories, Leicester University, LE1 9HN, Leicester, UK aut Robb Matthew Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK aut Shoolingin Jordan Peter Biochemistry Dept, University of Southampton, SO16 7PX, Southampton, UK aut Smith Alison Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK aut Planta Springer-Verlag 199/4(1996-08-01), 557-564 0032-0935 199:4<557 1996 199 425 https://doi.org/10.1007/BF00195187 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00195187 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Witty Michael Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK aut NATIONALLICENCE 700 1- Jones Russell Toxicology Unit, MRC Laboratories, Leicester University, LE1 9HN, Leicester, UK aut NATIONALLICENCE 700 1- Robb Matthew Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK aut NATIONALLICENCE 700 1- Shoolingin Jordan Peter Biochemistry Dept, University of Southampton, SO16 7PX, Southampton, UK aut NATIONALLICENCE 700 1- Smith Alison Department of Plant Sciences, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK aut NATIONALLICENCE 773 0- Planta Springer-Verlag 199/4(1996-08-01), 557-564 0032-0935 199:4<557 1996 199 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer