|
type |
Journal Article |
authors |
Schmidt, A. |
title |
D-Cysteine desulfhydrase from spinach |
journal |
Methods Enzymol |
Activity |
4.4.1.15 |
ui |
qwertok |
year |
(1987) |
volume |
143 |
number |
3 |
pages |
449-53. |
| |
abstract |
D-Cysteine desulfhydrase was prepd. from homogenized spinach leaves by polymin P and (NH4)2SO4 pptn., gel chromatog., DEAE-cellulose chromatog., and mol. sieving on Biogel A-1.5M. A 110-fold purifn. with 34% yield was obtained. The purified enzyme had a specific activity of 5.7 mmol H2S formed/mg protein/h. It was specific for D-cysteine and was not inhibited by 2 mM Mg2+, Ca2+, K+, Na+, or Al3+. The enzyme was assayed by measuring the formation of H2S from D-cysteine (H2S was detd. by a reaction that forms methylene blue). |
last changed |
2004/02/13 18:59 |
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