| Literature DB >> 2548475 |
G Schmalzing1, S Kröner, H Passow.
Abstract
Ouabain binding was studied in Xenopus laevis oocytes permeabilized by detergents. The behaviour of markers showed that 10 microM-digitonin selectively disrupts the plasma membrane. In the presence of ATP, oocytes permeabilized at 10 microM-digitonin bound no more ouabain molecules than were required to abolish active 86Rb+ uptake in the intact cells. However, the ouabain binding capacity increased approx. 2-fold when inner membranes were disrupted by SDS or excess digitonin, as judged from the accompanying release of the lysosomal marker beta-hexosaminidase. The results suggest that oocytes have a large internal pool of functional sodium pumps.Entities:
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Year: 1989 PMID: 2548475 PMCID: PMC1138682 DOI: 10.1042/bj2600395
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857