Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Alcides F. Rega"'
Autor:
Alcides F. Rega
This title was first published in 1986. It comprises contemporary knowledge of the calcium pump of plasma membranes and associated fields of research.
Autor:
Luis M. BREDESTON, Alcides F. REGA
Publikováno v:
Biochemical Journal. 361:355-361
Pre-steady-state phosphorylation and dephosphorylation of purified and phospholipid-depleted plasma-membrane Ca2+-ATPase (PMCA) solubilized in the detergent polyoxyethylene 10 lauryl ether were studied at 25°C. The time course of phosphorylation wit
Autor:
Alcides F. Rega, Luis M. Bredeston
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1420:57-62
Ca(2+)-ATPase of plasma membranes (PMCA) was isolated from either human or pig red cells by calmodulin-affinity chromatography and supplemented with phosphatidylcholine (PC). The specific activity of the purified PMCA diluted in media with detergent
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1324(1):85-90
A cDNA encoding a plasma membrane Ca2+ pump mutant V674P(ct120) was constructed and expressed in COS-1 cells. Immunoblots of transfected COS-1 membranes showed that the V674P(ct120) and the wild-type hPMCA4b(ct120) proteins were expressed at similar
Publikováno v:
Biochemical Journal. 315:673-677
The effects of 100 mM K+ on the partial reactions that take place during ATP hydrolysis on the calcium ion-dependent ATPase from plasma membrane (PM-Ca(2+)-ATPase) were studied at 37 degrees C on fragmented intact membranes from pig red cells by mean
Autor:
Alcides F. Rega, Claudio J. Herscher
Publikováno v:
Biochemistry. 35:14917-14922
Lanthanides are known to be effective inhibitors of the PMCa(2+)-ATPase. The effects of LaCl3 on the partial reactions that take place during ATP hydrolysis by the calcium-dependent ATPase from plasma membrane (PMCa(2+)-ATPase) were studied at 37 deg
Publikováno v:
Journal of Biological Chemistry. 269:10400-10406
The breakdown of phosphoenzyme (EP) of the Ca(2+)-ATPase from pig red blood cell membranes was studied at 37 degrees C by means of a rapid chemical quenching technique. When the enzyme was phosphorylated with [gamma-32P]ATP in media without added MgC
Publikováno v:
Journal of Biological Chemistry. 269:1051-1056
The maximum rate of phosphorylation (rm) of a highly purified Na,K-ATPase from red outer medulla of pig kidney was measured at 25 degrees C as a function of ATP concentration in media with Mg2+, Na+, and no K+. When rm was plotted as a function of th
Publikováno v:
Journal of Biological Chemistry. 267:6596-6601
Pre-steady-state phosphorylation of purified Na,K-ATPase from red outer medulla of pig kidney was studied at 25 degrees C and an ample range of [tau-32P]ATP concentrations. At 10 microM ATP phosphorylation followed simple exponential kinetics reachin