Properties and regulation of adenosine 5′-phosphosulfate sulfotransferase from suspension cultures of Nicotiana sylvestris

Jenni, B. E.; Brunold, Christian; Zrÿd, J. -P.; Lavanchy, P. (1980). Properties and regulation of adenosine 5′-phosphosulfate sulfotransferase from suspension cultures of Nicotiana sylvestris. Planta, 150(2), pp. 140-143. Springer 10.1007/BF00582357

Preview

Text 1980_Planta_150_140.pdf - Published Version Available under License Publisher holds Copyright. Download (445kB) | Preview

The properties and the regulation of adenosine 5′-phosphosulfate sulfotransferase extracted from cell suspension cultures ofNicotiana sylvestris was investigated. Optimal adenosine 5′-phosphosulfate sulfotransferase activity was obtained from the cells by extraction with 0.1 M tris-HCl, pH8.0, containing 2 M MgSO4 and 10 mM dithioerythritol. The K m for adenosine 5′-phosphosulfate in the sulfotransferase reaction was about 11 μM. Adenosine 5′-phosphosulfate in concentrations above 50 μM were inhibitory. The extratable adenosine 5′-phosphosulfate sulfotransferase activity decreased during cultivation with sulfate as the sole sulfur source, but after about 3 days it reached a constant level (50 to 100 nmol activated sulfate transferred h-1 mg-1 protein) which was maintained for at least 24 h. Addition of 0.5 mM cysteine to the culture medium decreased the extractable adenosine 5′-phosphosulfate sulfotransferase activity and blocked growth completely. With 0.1 mM cysteine an enzyme level of about 10% of the initial value was reached within 6 to 12 h without significant inhibition of growth. The added cysteine was absorbed rapidly and after 24 h cysteine could no longer be detected in the medium. Before the cysteine was completely depleted, the activity of adenosine 5′-phosphosulfate sulfotransferase started to increase, reaching ultimately a level which was comparable to the initial value.

Interest & Impact

Downloads

19 since deposited on 13 Jun 2018
18 in the past 12 months

Citations

5 Citations in Web of Science ®
6 Citations in Scopus

Search

in Google Scholar™

Services

Actions (login required)

Edit item

Actions (login required)

Edit item