Ferrochelatase: Isolation and purification via affinity chromatography

1980 ◽  
Vol 96 (2) ◽  
pp. 777-784 ◽  
Author(s):  
K. Mailer ◽  
R. Poulson ◽  
D. Dolphin ◽  
A.D. Hamilton
2007 ◽  
Vol 50 (18) ◽  
pp. 4329-4339 ◽  
Author(s):  
Sebastian Knör ◽  
Alexey V. Khrenov ◽  
Burkhardt Laufer ◽  
Evgueni L. Saenko ◽  
Charlotte A. E. Hauser ◽  
...  

1987 ◽  
Vol 241 (1) ◽  
pp. 71-74 ◽  
Author(s):  
F Cadet ◽  
J C Meunier ◽  
N Ferté

Higher-plant sedoheptulose-1,7-bisphosphatase was isolated and purified over 200-fold from spinach (Spinacia oleracea) chloroplast stromal extracts to apparent electrophoretic homogeneity by DEAE-Fractogel, molecular sieving on Sephadex G-200 and Blue B dye-matrix affinity chromatography. It is a protein of Mr 66,000, made up of two apparently identical subunits (Mr 35,000). The enzyme is activated by reduced thioredoxin fb in the presence of dithiothreitol. Its specificity towards sedoheptulose 1,7-bisphosphate versus fructose 1,6-bisphosphate is high, but not absolute.


Life Sciences ◽  
1985 ◽  
Vol 36 (11) ◽  
pp. 1075-1085 ◽  
Author(s):  
Tae Mook Cho ◽  
Bang-Lun Ge ◽  
Horace H. Loh

2011 ◽  
Vol 1218 (5) ◽  
pp. 706-710 ◽  
Author(s):  
Andrea Mönster ◽  
Oliver Hiller ◽  
Daniela Grüger ◽  
Rainer Blasczyk ◽  
Cornelia Kasper

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