Article
Purification and characterization of a 14-kilodalton protein that is bound to the surface of polyhydroxyalkanoic acid granules in Rhodococcus ruber.
Journal of bacteriology - 1 Jul 1994
Pieper-Fürst U, Madkour M H, Mayer F, Steinbüchel A
Abstract excerpt
The N-terminal amino acid sequence of the polyhydroxyalkanoic acid (PHA) granule-associated M(r)-15,500 protein of Rhodococcus ruber (the GA14 protein) was analyzed. The sequence revealed that the corresponding structural gene is represented by open reading frame 3, encoding a protein with a calculated M(r) of 14,175 which was recently localized downstream of the PHA synthase gene (U. Pieper and A. Steinbüchel,...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Cytoplasmic Granules
- Hydroxy Acids
- Membrane Proteins
- Microscopy, Immunoelectron
- Molecular Sequence Data
- Molecular Weight
- Mutation