|
type |
Journal Article |
authors |
Masuda, T.; Sakamoto, M.; Nishizaki, I.; Hayashi, H.; Yamamoto, M.; Wada, H. |
title |
Affinity purification and characterization of serine hydroxymethyltransferases from rat liver |
journal |
J Biochem (Tokyo) |
Activity |
2.1.2.1 |
ui |
87250349 |
year |
(1987) |
volume |
101 |
number |
3 |
pages |
643-52. |
| |
keywords |
Animal |
abstract |
A rapid and simple method was developed for the purification of serine hydroxymethyltransferases [EC 2.1.2.1]. The procedure involved ammonium sulfate precipitation, DEAE-cellulose column chromatography and affinity chromatography on an L-adsorbent. Through this procedure the cytosolic enzyme (s-SHMT) was purified 1,650-fold, and the mitochondrial enzyme (m-SHMT) 1,730-fold, with a yield of more than 30% in both cases. Both preparations gave a single band with a Mr of 54,000 on SDS-PAGE. The native enzymes both contained 4 mol of pyridoxal phosphate/mol of enzyme, and showed a Mr value of 220,000 on gel filtration, indicating a tetrameric structure. Several other properties of the enzymes were also studied. |
last changed |
2002/11/04 17:41 |
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