|
type |
Journal Article |
authors |
Hayasaka, K.; Kochi, H.; Hiraga, K.; Kikuchi, G. |
title |
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 |
J Biochem (Tokyo) |
Activity |
1.4.4.2 |
ui |
81093892 |
year |
(1980) |
volume |
88 |
number |
4 |
pages |
1193-9. |
| |
keywords |
Amino Acid Oxidoreductases/isolation & purification/*metabolism |
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. |
last changed |
2002/11/04 17:41 |
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