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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/15314
Title: The relationship of phosphorylation of membrane proteins with the osmotic fragility and filterability of Plasmodium berghei-infected mouse erythrocytes
Authors: Yongyuth Yuthavong
Temduang Limpaiboon
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 29-Jul-1987
Citation: BBA - Molecular Cell Research. Vol.929, No.3 (1987), 278-287
Abstract: Membrane from Plasmodium berghei-infected mouse erythrocytes showed a pattern of protein phosphorylation which was substantially altered from the normal pattern, with an increase in the phosphorylation of the protein with an apparent molecular weight of 43 000 (M 43), which increased from undetectable in uninfected cells to a maximum in the mature trophozoite stage. Phosphorylation levels of this and other minor bands were strongly correlated with osmotic fragility and filterability. The level of M 43 phosphorylation in membranes from cells which remained intact in a hypotonic medium was 3.82 ± 0.59-times that of lysed cells, compared with the value of 0.76 ± 0.07 calculated from distribution alone. Results found when intact erythrocytes were phosphorylated by incubation with [ 32 P]P i prior to partial lysis were similar to those found when membranes from the lysed and unlysed fractions were subsequently phosphorylated with [γ- 32 P]ATP. Infected erythrocytes which could pass repeatedly through 3-μm polycarbonate filters had a much higher phosphorylation level for the M 43 region than whole infected cells with similar parasitemia and stage distribution. The phosphorylation change could play a role in the control of osmotic and mechanical properties of the infected erythrocytes during maturation. © 1987.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0023667518&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/15314
ISSN: 01674889
Appears in Collections:Scopus 1969-1990

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