Binding of /sup 14/C-5-aminolevulinic acid to a stromal protein from developing pea chloroplasts
/sup 14/-5-Aminolevulinic acid (/sup 14/C-ALA) binds to a stromal protein with an apparent molecular weight of 42-43 KD on LDS and non-denaturing gels. The reaction is rapid. Binding is inhibited by sulfhydryl reagents, mM concentrations of levulinic, dihydroxy heptanoic acids and gabaculine, 10 ..mu..M N-methylprotoporphyrin. Dicarboxilic acids, such as deltaKG, Glu, OAA, do not inhibit. Chloramphenicol, ATP, protoporphyrin, anoxia, light, darkness have no effect. The product, once formed, is stable to treatment with 5% conc. HCl in cold acetone. It can be chased in a second incubation with unlabeled ALA, but not with levulinic acid. No activity was detected in the subplastidic membrane fractions. Western blot analysis failed to reveal any homology between the labeled protein and either cytochrome for ALA dehydratase. This ALA-binding protein was not formed in chloroplasts isolated from fully expanded pea leaves. Therefore, it is deemed likely to participate in ALA metabolism during chloroplast development.
- Research Organization:
- Univ. of California, Davis
- OSTI ID:
- 5653473
- Report Number(s):
- CONF-8707108-
- Journal Information:
- Plant Physiol., Suppl.; (United States), Vol. 83:4; Conference: Annual meeting of the American Society of Plant Physiologists, St. Louis, MO, USA, 19 Jul 1987
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
AMINOLEVULINIC ACID
METABOLISM
CHLOROPLASTS
CHEMICAL COMPOSITION
CARBON 14 COMPOUNDS
ELECTROPHORESIS
HYBRIDIZATION
LEAVES
LEVULINIC ACID
PISUM
PROTEINS
TRACER TECHNIQUES
AMINO ACIDS
BACTERIA
CARBOXYLIC ACIDS
CELL CONSTITUENTS
ISOTOPE APPLICATIONS
KETO ACIDS
LABELLED COMPOUNDS
LEGUMINOSAE
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PLANTS
RHIZOBIUM
550201* - Biochemistry- Tracer Techniques