Purification and properties of glycine decarboxylase, a component of the glycine cleavage system, from rat liver mitochondria and immunochemical comparison of this enzyme from various sources.
Journal of biochemistry
confidence
Key findings
Purified glycine decarboxylase (P-protein) from rat liver mitochondria; biochemical and immunological characterization across species; no clinical/biological endpoints reported.
View source on PubMed (PMID 6778858) ↗
- Sample size
- Not reported
- Population
- Rat liver mitochondria (in vitro purification); immunological comparison across species
- Dosing
- Not applicable
- Duration
- Not reported
- Route
- Not applicable
- Blinding
- not_reported
- Controls
- none
- Drug class
- amino acid
Full abstract
Glycine decarboxylase, tentatively called P-protein as a constituent of the glycine cleavage system, was purified to near homogeneity from rat liver mitochondria. The purified P-protein was a homodimer with a molecular weight of about 210,000, consisting of identical subunits with a molecular weight of 105,000. In the exchange reaction of the carboxyl carbon of glycine wih CO2 catalyzed by the purified P-protein in the presence of H-protein, the pH optimum was 6.7, Km for glycine was 6.6 mM, and Km for H-protein was 7.4 microM. A specific rabbit antibody against the purified rat liver P-protein was prepared. Ouchterlony double diffusion analysis and immunoinhibition experiments using this antibody revealed immunological cross-reactivity among the P-proteins from various species of animals such as carp, frog, snake, chicken, bovine, and human, suggesting a quite conservative evolution of the glycine cleavage system.