K+-p-nitrophenylphosphatase activity in rat brain and liver

Title:

K+-p-nitrophenylphosphatase activity in rat brain and liver

Creator:

Monika Ďurfinová, Marta Brechtlová, Branislav Líška, and Želmíra Barošková

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:7f477a7b-e123-4732-a988-405ec9e110ce
uuid:7f477a7b-e123-4732-a988-405ec9e110ce

Subject:

Biochemie. Molekulární biologie. Biofyzika, biochemie, mozek, játra, biochemistry, brain, liver, K+-ATPase, K+-p-nitrophenylphospatase, 2, and 577

Type:

article, články, model:article, and TEXT

Format:

print

Description:

K+-p-nitrophenylphosphatase (K+pNPPase) is the enzyme, which is considered to be involved in K+-dependent hydrolysis of the phosphoenzyme in the reaction cycle of Na+, K+-ATPase. The aim of our present study was to characterize some features of K+pNPPase in homogenates of the rat brain and liver. We determined p-nitrophenylphosphatase (pNPPase) activity in the presence of various ion combinations (Mg 2++K+, Mg2+, K+). We found a higher total pNPPase activity in the brain (0.8±0.079 nkat/mg protein) than in the liver (0.08±0.01 nkat/mg protein). Contrary to the liver, the main part of the total brain activity was K+-dependent. The activity of K+pNPPase was significantly higher in cerebral cortex homogenates (0.86±0.073 nkat/mg protein) in comparison to those of the whole brain (0.57±0.075 nkat/mg protein). The specific K+pNPPase activity was two times higher in the isolated pellet fraction (0.911±0.07 nkat/mg protein), rich in synaptosomes, compared to the whole brain homogenate (0.57±0.075 nkat/mg protein). Our results demonstrate the high activity of K+pNPPase in the brain tissue and its distribution mainly into the pellet fraction, what might indicate a possible role of K+pNPPase in specific structures of the brain, e.g. in synaptosomes., M. Ďurfinová, M. Brechtlová, B. Líška, Ž. Barošková., and Obsahuje seznam literatury

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2009 Volume:58 | Number:1

Harvested from:

CDK

Metadata only:

false