1. Control Mechanisms at the Level of FDP-Aldolases in Algae
- Author
-
T. Cremona
- Subjects
chemistry.chemical_classification ,Euglena gracilis ,ved/biology ,Dimer ,ved/biology.organism_classification_rank.species ,Plant Science ,Biology ,biology.organism_classification ,chemistry.chemical_compound ,Amino acid analysis ,Monomer ,Enzyme ,Biochemistry ,chemistry ,Algae ,Ecology, Evolution, Behavior and Systematics - Abstract
The FDP-aldolase I from Euglena gracilis is a four-chain enzyme, as shown by the amino acid analysis of the C and N terminals. The protein is dissociated by acid pH to a monomer. The reassociation-dissociation process goes through a dimer stage. The enzyme, inhibited either by mercurials or by ATP, is dissociated to a dimer. This process is readly reversible either by mercaptoethanol and by AMP.
- Published
- 1968
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