Article
Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli.
Plant molecular biology - 1 May 1991
Lal S K, Johnson S, Conway T, Kelley P M
Abstract excerpt
A cDNA encoding maize enolase (2-phospho-D-glycerate hydrolase) was purified by functional genetic complementation using an enolase deficient mutant of Escherichia coli, DF261. This cDNA, pZM245, was characterized by restriction mapping and DNA sequence analysis. The cDNA contained an open reading frame encoding a protein of 446 amino acids with a high degree of similarity to enolase sequences from other...
Topics
- Amino Acid Sequence
- Base Sequence
- Blotting, Northern
- Blotting, Southern
- DNA
- Escherichia coli
- Genetic Complementation Test
- Molecular Sequence Data
- Mutation
- Phosphopyruvate Hydratase
- Plasmids