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Localisation of β‐oxidation enzymes in peroxisomes of rice coleoptiles
Author(s) -
Pistelli Laura,
Rascio Nicoletta,
Bellis Luigi,
Alpi Amedeo
Publication year - 1989
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1989.tb05623.x
Subject(s) - peroxisome , coleoptile , thiolase , biochemistry , biology , oxidase test , enzyme , microbody , oryza sativa , dehydrogenase , cell fractionation , mitochondrion , gene
Enzymes of the β‐oxidation pathway in rice ( Oryza sativa L., cv. Arborio) coleoptiles were investigated. The coleoptiles contain acyl‐CoA oxidase (EC 1.3.99.3), 3‐hydroxyacyl‐CoA dehydrogenase (EC 1.1.1.35), enoyl‐CoA hydratase (EC 4.2.1.17) and thiolase (EC 2.3.1.9). Analysis of coleoptile homogenates by sucrose density fractionation showed a preferential distribution of these enzymes in the unspecialized peroxisomes. The enzymatic activity found in the mitochondrial fraction was due to peroxisomal contamination since electron micrographs show the peroxisomes to be intact and pure whereas the mitochondrial fraction was contaminated by other organelles. It appears that the β‐oxidation pathway is localized in the unspecialized peroxisomes of rice coleoptiles, extending the number of plant species in which such a localization has been observed.