Properties and regulation of adenosine 5′-phosphosulfate sulfotransferase from suspension cultures of Nicotiana sylvestris
Publisher DOI
Abstract
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.
Date Issued
1980-01
Publication Type
Article
Subject(s)
Subjects
adenosine 5′-phosphosulfate sulfotransferase
•
cell suspension culture
•
cysteine
•
enzyme regulation
•
Nicotiana
Language(s)
en
Author(s)
Jenni, B. E. | |
Zrÿd, J. -P. | |
Lavanchy, P. |
Additional Credits
Journal
Planta
Publisher
Springer
ISSN
0032-0935
Access(Rights)
open.access