Preparation and partial characterization of a soluble site-to-site directed enzyme complex composed of alcohol dehydrogenase and lactate dehydrogenase

1987 ◽  
Vol 12 (2) ◽  
pp. 91-105 ◽  
Author(s):  
Nils Siegbahn ◽  
Mats-Olle Maånsson ◽  
Klaus Mosbach
1983 ◽  
Vol 213 (2) ◽  
pp. 547-550 ◽  
Author(s):  
P Julià ◽  
J Farrés ◽  
X Parés

Homogeneous alcohol dehydrogenase (ADH) from rat retina was obtained by chromatography on DEAE-Sepharose and AMP-hexane-Sepharose. The enzyme is a dimer of Mr congruent to 80000 and oxidizes ethanol using NAD+ as a cofactor. Careful activity determinations demonstrate unambiguously that rat retina ADH is active with retinol as a substrate. This result opens the question about the role of retina ADH in the visual cycle.


1994 ◽  
Vol 24 (1) ◽  
pp. 87-94 ◽  
Author(s):  
G. Gasperi ◽  
D. Kafetzopoulos ◽  
A. Christodoulidou ◽  
V. Bouriotis ◽  
C. Savakis

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