title: Immunological cross-reactivity between proton-pumping inorganic pyrophosphatases of widely phylogenic separated species.
abstract: Immunological cross-reactivity among three types of inorganic pyrophosphatases, that is, the proton pumping inorganic pyrophosphate synthase (H(+)-PPi synthase) and the soluble inorganic pyrophosphatase, both from Rhodospirillum rubrum, and the vacuolar membrane inorganic pyrophosphatase (H(+)-PPase) from mung bean (Vigna radiata), were examined by means of immunoblot analyses. Antibodies raised against the mung bean H(+)-PPase cross-reacted with the H(+)-PPi synthase from R. rubrum but not with the soluble PPase from R. rubrum. N,N'-dicyclohexylcarbodiimide (DCCD), which inhibits both synthesis and hydrolysis of PPi catalysed by purified and chromatophore H(+)-PPi synthase, binds to the enzyme as shown by fluorography of [14C]DCCD labelling. These results suggest that the R. rubrum H(+)-PPase share close structural similarities with the vacuolar H(+)-PPase from Mung bean.
authors.affiliation: Department of Biochemistry, University of Stockholm, Sweden.
authors.forename: B F
authors.initials: BF
authors.lastname: Nore
authors.forename: Y
authors.initials: Y
authors.lastname: Sakai-Nore
authors.forename: M
authors.initials: M
authors.lastname: Maeshima
authors.forename: M
authors.initials: M
authors.lastname: Baltscheffsky
authors.forename: P
authors.initials: P
authors.lastname: Nyrén
mesh_terms: D015153:Blotting, Western; D002846:Chromatography, Affinity; D003429:Cross Reactions; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D043564:Inorganic Pyrophosphatase; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D011485:Protein Binding; D011755:Pyrophosphatases / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D014617:Vacuoles / Q000201:enzymology
chemical_list: D004024:Dicyclohexylcarbodiimide; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase