Title : P-glycoprotein. ATP hydrolysis by the N-terminal nucleotide-binding domain.

Pub. Date : 1992 Mar 5

PMID : 1347041






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Two ATP-binding domains are found in members of the family of ATP-dependent transport proteins, which includes P-glycoprotein and cystic fibrosis transmembrane conductance regulator. Adenosine Triphosphate ATP binding cassette subfamily B member 1 Homo sapiens
2 Two ATP-binding domains are found in members of the family of ATP-dependent transport proteins, which includes P-glycoprotein and cystic fibrosis transmembrane conductance regulator. Adenosine Triphosphate ATP binding cassette subfamily B member 1 Homo sapiens
3 To investigate the involvement of the two ATP-binding domains in the ATPase activity of P-glycoprotein, full-length and the 5"-half of human MDR1 cDNA, which encodes P-glycoprotein, were fused with the Escherichia coli lacZ gene and expressed in NIH3T3 cells. Adenosine Triphosphate ATP binding cassette subfamily B member 1 Homo sapiens
4 To investigate the involvement of the two ATP-binding domains in the ATPase activity of P-glycoprotein, full-length and the 5"-half of human MDR1 cDNA, which encodes P-glycoprotein, were fused with the Escherichia coli lacZ gene and expressed in NIH3T3 cells. Adenosine Triphosphate ATP binding cassette subfamily B member 1 Homo sapiens
5 Immunoprecipitated full-length P-glycoprotein beta-galactosidase showed ATPase activity with apparent specific activity of 180 nmol/mg/min, a value higher than previously reported, in the presence of phospholipids, suggesting that stabilization of the transmembrane domains is necessary for ATP hydrolysis. Adenosine Triphosphate ATP binding cassette subfamily B member 1 Homo sapiens
6 N-terminal half P-glycoprotein-beta-galactosidase also showed ability to hydrolyze ATP but with slightly lower specific activity. Adenosine Triphosphate ATP binding cassette subfamily B member 1 Homo sapiens