[Catalytic characteristics of 5'-nucleotidase in the structure of cell membrane rafts in smooth muscles].
5'-nucleotidase (EN 3.1.3.5) is widely distributed enzyme occurring in vertebrate, bacterial and plant cells. The main physiological function of 5'-nucleotidase is hydrolysis of 5'-AMP to adenosine and Pi. It was found that the detergent-insoluble membrane domains (rafts) are enriched by proteins possessing high 5'-AMPase activity. This study is aimed to investigate some physical and chemical properties of 5'-nucleotidase, which is present in detergent insoluble membrane domains isolated from pig stomach and lung. It was shown for the first time that catalytic properties of the raft-associated 5'-nucleotidase and of the pure enzyme described in literature differ. Our results demonstrate that the greatest activity of the raft-associated enzyme takes place in the physiological conditions contrary to the pure enzyme. Our data suggest that such changes of 5'-nucleotidase catalytic activity might be due to the disruption of its interaction with membrane rafts.
Danylova
V M
VM
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Taras Shevchenko Kyiv National University, Kyiv. valdan@biochem.kiev.ua
Andrukhova
O V
OV
Babiĭchuk
V S
VS
Andrukhov
O Ia
OIa
Babiĭchuk
E B
EB
D015720:5'-Nucleotidase / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D066298:In Vitro Techniques; D008168:Lung / Q000201:enzymology; D021962:Membrane Microdomains / Q000201:enzymology*; D009130:Muscle, Smooth / Q000201:enzymology*; D013270:Stomach / Q000201:enzymology; D013379:Substrate Specificity; D013552:Swine
D015720:5'-Nucleotidase