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