|
type |
Journal Article |
authors |
Masada, M.; Fukushima, K.; Tamura, G. |
title |
Cysteine synthase from rape leaves |
journal |
J Biochem (Tokyo) |
Activity |
2.5.1.47 |
ui |
76005462 |
year |
(1975) |
volume |
77 |
number |
5 |
pages |
1107-15. |
| |
keywords |
Chromatography, Gel |
abstract |
Cysteine synthase [O-Acetyl-L-serine acetate-lyase (adding hydrogen- sulfide) EC 4.2.99.8] has been highly purified from the extract of rape, Brassica chinensis var. Komatsuna. The purified preparation appeared to be homogeneous on Sephadex G-100 gel filtration and dodecylsulfate-polyacrylamide gel electrophoresis, showing a molecular weight of about 62,000. The latter method also suggested that this enzyme was composed of two identical subunits. The enzyme contained 2 moles of pyridoxal phosphate per mole of enzyme. |
last changed |
2003/03/17 14:53 |
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